Target Binding Site Detail

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Target General Information
Ligand General Information
Drug Binding Sites of Target
References
Target General Information  Top
Target ID T55654 Target Info
Target Name cAMP-dependent chloride channel (CFTR)
Synonyms cAMPdependent chloride channel; Cystic fibrosis transmembrane conductance regulator; Channel conductancecontrolling ATPase; ATPbinding cassette subfamily C member 7; ATP-binding cassette sub-family C member 7; ABCC7
Target Type Successful Target
Gene Name CFTR
Biochemical Class ABC transporter
UniProt ID
CFTR_HUMAN
Ligand General Information  Top
Ligand Name Adenosine triphosphate Ligand Info
Canonical SMILES C1=NC(=C2C(=N1)N(C=N2)C3C(C(C(O3)COP(=O)(O)OP(=O)(O)OP(=O)(O)O)O)O)N
InChI 1S/C10H16N5O13P3/c11-8-5-9(13-2-12-8)15(3-14-5)10-7(17)6(16)4(26-10)1-25-30(21,22)28-31(23,24)27-29(18,19)20/h2-4,6-7,10,16-17H,1H2,(H,21,22)(H,23,24)(H2,11,12,13)(H2,18,19,20)/t4-,6-,7-,10-/m1/s1
InChIKey ZKHQWZAMYRWXGA-KQYNXXCUSA-N
PubChem Compound ID 5957
Drug Binding Sites of Target  Top
PDB ID: 7SVD      The complex of phosphorylated human cystic fibrosis transmembrane conductance regulator (CFTR) with ATP/Mg and Lumacaftor (VX-809)
Method Electron microscopy Resolution 2.70 Å Mutation Yes [1]
PDB Sequence
MQRSPLEKAS
10
VVSKLFFSWT
20
RPILRKGYRQ
30
RLELSDIYQI
40
PSVDSADNLS
50

EKLEREWDRE
60
LASKKNPKLI
70
NALRRCFFWR
80
FMFYGIFLYL
90
GEVTKAVQPL
100

LLGRIIASYD
110
PDNKEERSIA
120
IYLGIGLCLL
130
FIVRTLLLHP
140
AIFGLHHIGM
150

QMRIAMFSLI
160
YKKTLKLSSR
170
VLDKISIGQL
180
VSLLSNNLNK
190
FDEGLALAHF
200

VWIAPLQVAL
210
LMGLIWELLQ
220
ASAFCGLGFL
230
IVLALFQAGL
240
GRMMMKYRDQ
250

RAGKISERLV
260
ITSEMIENIQ
270
SVKAYCWEEA
280
MEKMIENLRQ
290
TELKLTRKAA
300

YVRYFNSSAF
310
FFSGFFVVFL
320
SVLPYALIKG
330
IILRKIFTTI
340
SFCIVLRMAV
350

TRQFPWAVQT
360
WYDSLGAINK
370
IQDFLQKQEY
380
KTLEYNLTTT
390
EVVMENVTAF
400

WEEGFGELFG
437
TPVLKDINFK
447
IERGQLLAVA
457
GSTGAGKTSL
467
LMVIMGELEP
477

SEGKIKHSGR
487
ISFCSQFSWI
497
MPGTIKENII
507
FGVSYDEYRY
517
RSVIKACQLE
527

EDISKFAEKD
537
NIVLGEGGIT
547
LSGGQRARIS
557
LARAVYKDAD
567
LYLLDSPFGY
577

LDVLTEKEIF
587
ESCVCKLMAN
597
KTRILVTSKM
607
EHLKKADKIL
617
ILHEGSSYFY
627

GTFSELQNLW
846
NTYLRYITVH
856
KSLIFVLIWC
866
LVIFLAEVAA
876
SLVVLWLLGN
886

TPSYAVIITS
909
TSSYYVFYIY
919
VGVADTLLAM
929
GFFRGLPLVH
939
TLITVSKILH
949

HKMLHSVLQA
959
PMSTLNTLKA
969
GGILNRFSKD
979
IAILDDLLPL
989
TIFDFIQLLL
999

IVIGAIAVVA
1009
VLQPYIFVAT
1019
VPVIVAFIML
1029
RAYFLQTSQQ
1039
LKQLESEGRS
1049

PIFTHLVTSL
1059
KGLWTLRAFG
1069
RQPYFETLFH
1079
KALNLHTANW
1089
FLYLSTLRWF
1099

QMRIEMIFVI
1109
FFIAVTFISI
1119
LTTGEGEGRV
1129
GIILTLAMNI
1139
MSTLQWAVNS
1149

SIDVDSLMRS
1159
VSRVFKFIDM
1169
PTEGIWPSGG
1208
QMTVKDLTAK
1218
YTEGGNAILE
1228

NISFSISPGQ
1238
RVGLLGRTGS
1248
GKSTLLSAFL
1258
RLLNTEGEIQ
1268
IDGVSWDSIT
1278

LQQWRKAFGV
1288
IPQKVFIFSG
1298
TFRKNLDPYE
1308
QWSDQEIWKV
1318
ADEVGLRSVI
1328

EQFPGKLDFV
1338
LVDGGCVLSH
1348
GHKQLMCLAR
1358
SVLSKAKILL
1368
LDQPSAHLDP
1378

VTYQIIRRTL
1388
KQAFADCTVI
1398
LCEHRIEAML
1408
ECQQFLVIEE
1418
NKVRQYDSIQ
1428

KLLNERSLFR
1438
QAISPSDRVK
1448
LFP
Residue
Distance (Å)
ASP173
4.773
TRP401
3.780
VAL440
4.066
SER459
4.052
THR460
2.898
GLY461
2.958
ALA462
3.236
GLY463
2.735
LYS464
2.842
THR465
3.187
SER466
3.273
GLN493
3.314
PHE533
3.776
ILE546
3.637
THR547
3.276
LEU548
4.145
SER549
3.507
GLY550
3.776
GLY551
3.089
GLN552
3.445
TYR577
4.413
ASN965
3.909
Residue
Distance (Å)
TYR1219
3.668
ILE1226
3.664
ARG1245
3.764
THR1246
2.840
GLY1247
2.706
SER1248
3.060
GLY1249
2.641
LYS1250
2.931
SER1251
3.262
THR1252
3.282
GLN1291
3.388
GLN1330
3.968
PHE1331
4.846
CYS1344
3.445
VAL1345
3.090
LEU1346
4.397
SER1347
3.248
HIS1348
3.404
GLY1349
3.469
HIS1350
4.078
HIS1402
3.103
PDB ID: 7SV7      The complex of phosphorylated human cystic fibrosis transmembrane conductance regulator (CFTR) with ATP/Mg and Tezacaftor (VX-661)
Method Electron microscopy Resolution 3.80 Å Mutation Yes [1]
PDB Sequence
MQRSPLEKAS
10
VVSKLFFSWT
20
RPILRKGYRQ
30
RLELSDIYQI
40
PSVDSADNLS
50

EKLEREWDRE
60
LASKKNPKLI
70
NALRRCFFWR
80
FMFYGIFLYL
90
GEVTKAVQPL
100

LLGRIIASYD
110
PDNKEERSIA
120
IYLGIGLCLL
130
FIVRTLLLHP
140
AIFGLHHIGM
150

QMRIAMFSLI
160
YKKTLKLSSR
170
VLDKISIGQL
180
VSLLSNNLNK
190
FDEGLALAHF
200

VWIAPLQVAL
210
LMGLIWELLQ
220
ASAFCGLGFL
230
IVLALFQAGL
240
GRMMMKYRDQ
250

RAGKISERLV
260
ITSEMIENIQ
270
SVKAYCWEEA
280
MEKMIENLRQ
290
TELKLTRKAA
300

YVRYFNSSAF
310
FFSGFFVVFL
320
SVLPYALIKG
330
IILRKIFTTI
340
SFCIVLRMAV
350

TRQFPWAVQT
360
WYDSLGAINK
370
IQDFLQKQEY
380
KTLEYNLTTT
390
EVVMENVTAF
400

WEEGFGELFG
437
TPVLKDINFK
447
IERGQLLAVA
457
GSTGAGKTSL
467
LMVIMGELEP
477

SEGKIKHSGR
487
ISFCSQFSWI
497
MPGTIKENII
507
FGVSYDEYRY
517
RSVIKACQLE
527

EDISKFAEKD
537
NIVLGEGGIT
547
LSGGQRARIS
557
LARAVYKDAD
567
LYLLDSPFGY
577

LDVLTEKEIF
587
ESCVCKLMAN
597
KTRILVTSKM
607
EHLKKADKIL
617
ILHEGSSYFY
627

GTFSELQNLW
846
NTYLRYITVH
856
KSLIFVLIWC
866
LVIFLAEVAA
876
SLVVLWLLGN
886

TPSYAVIITS
909
TSSYYVFYIY
919
VGVADTLLAM
929
GFFRGLPLVH
939
TLITVSKILH
949

HKMLHSVLQA
959
PMSTLNTLKA
969
GGILNRFSKD
979
IAILDDLLPL
989
TIFDFIQLLL
999

IVIGAIAVVA
1009
VLQPYIFVAT
1019
VPVIVAFIML
1029
RAYFLQTSQQ
1039
LKQLESEGRS
1049

PIFTHLVTSL
1059
KGLWTLRAFG
1069
RQPYFETLFH
1079
KALNLHTANW
1089
FLYLSTLRWF
1099

QMRIEMIFVI
1109
FFIAVTFISI
1119
LTTGEGEGRV
1129
GIILTLAMNI
1139
MSTLQWAVNS
1149

SIDVDSLMRS
1159
VSRVFKFIDM
1169
PTEGIWPSGG
1208
QMTVKDLTAK
1218
YTEGGNAILE
1228

NISFSISPGQ
1238
RVGLLGRTGS
1248
GKSTLLSAFL
1258
RLLNTEGEIQ
1268
IDGVSWDSIT
1278

LQQWRKAFGV
1288
IPQKVFIFSG
1298
TFRKNLDPYE
1308
QWSDQEIWKV
1318
ADEVGLRSVI
1328

EQFPGKLDFV
1338
LVDGGCVLSH
1348
GHKQLMCLAR
1358
SVLSKAKILL
1368
LDQPSAHLDP
1378

VTYQIIRRTL
1388
KQAFADCTVI
1398
LCEHRIEAML
1408
ECQQFLVIEE
1418
NKVRQYDSIQ
1428

KLLNERSLFR
1438
QAISPSDRVK
1448
LFP
Residue
Distance (Å)
TRP401
3.370
VAL440
4.187
SER459
4.278
THR460
2.812
GLY461
3.193
ALA462
4.733
GLY463
3.477
LYS464
2.503
THR465
2.812
SER466
3.042
GLN493
2.738
LYS532
4.938
PHE533
3.582
ILE546
4.068
THR547
3.196
LEU548
3.939
SER549
3.243
GLY550
3.746
GLY551
2.775
GLN552
3.074
TYR577
4.177
ASN965
3.804
TYR1219
3.309
Residue
Distance (Å)
ILE1226
4.057
ARG1245
4.124
THR1246
3.534
GLY1247
3.220
SER1248
3.275
GLY1249
3.437
LYS1250
2.801
SER1251
2.771
THR1252
3.028
GLN1291
3.010
VAL1327
4.665
GLN1330
3.781
PHE1331
4.464
CYS1344
3.514
VAL1345
2.906
LEU1346
3.995
SER1347
3.715
HIS1348
4.150
GLY1349
3.621
HIS1350
3.973
ASP1370
4.772
HIS1402
3.523
PDB ID: 8EIO      The complex of phosphorylated human delta F508 cystic fibrosis transmembrane conductance regulator (CFTR) with elexacaftor (VX-445), lumacaftor (VX-809) and ATP/Mg
Method Electron microscopy Resolution 2.80 Å Mutation Yes [2]
PDB Sequence
MQRSPLEKAS
10
VVSKLFFSWT
20
RPILRKGYRQ
30
RLELSDIYQI
40
PSVDSADNLS
50

EKLEREWDRE
60
LASKKNPKLI
70
NALRRCFFWR
80
FMFYGIFLYL
90
GEVTKAVQPL
100

LLGRIIASYD
110
PDNKEERSIA
120
IYLGIGLCLL
130
FIVRTLLLHP
140
AIFGLHHIGM
150

QMRIAMFSLI
160
YKKTLKLSSR
170
VLDKISIGQL
180
VSLLSNNLNK
190
FDEGLALAHF
200

VWIAPLQVAL
210
LMGLIWELLQ
220
ASAFCGLGFL
230
IVLALFQAGL
240
GRMMMKYRDQ
250

RAGKISERLV
260
ITSEMIENIQ
270
SVKAYCWEEA
280
MEKMIENLRQ
290
TELKLTRKAA
300

YVRYFNSSAF
310
FFSGFFVVFL
320
SVLPYALIKG
330
IILRKIFTTI
340
SFCIVLRMAV
350

TRQFPWAVQT
360
WYDSLGAINK
370
IQDFLQKQEY
380
KTLEYNLTTT
390
EVVMENVTAF
400

WEGTPVLKDI
444
NFKIERGQLL
454
AVAGSTGAGK
464
TSLLMVIMGE
474
LEPSEGKIKH
484

SGRISFCSQF
494
SWIMPGTIKE
504
NIIGVSYDEY
515
RYRSVIKACQ
525
LEEDISKFAE
535

KDNIVLGEGG
545
ITLSGGQRAR
555
ISLARAVYKD
565
ADLYLLDSPF
575
GYLDVLTEKE
585

IFESCVCKLM
595
ANKTRILVTS
605
KMEHLKKADK
615
ILILHEGSSY
625
FYGTFSELQN
635

LWNTYLRYIT
854
VHKSLIFVLI
864
WCLVIFLAEV
874
AASLVVLWLL
884
GSYAVIITST
910

SSYYVFYIYV
920
GVADTLLAMG
930
FFRGLPLVHT
940
LITVSKILHH
950
KMLHSVLQAP
960

MSTLNTLKAG
970
GILNRFSKDI
980
AILDDLLPLT
990
IFDFIQLLLI
1000
VIGAIAVVAV
1010

LQPYIFVATV
1020
PVIVAFIMLR
1030
AYFLQTSQQL
1040
KQLESEGRSP
1050
IFTHLVTSLK
1060

GLWTLRAFGR
1070
QPYFETLFHK
1080
ALNLHTANWF
1090
LYLSTLRWFQ
1100
MRIEMIFVIF
1110

FIAVTFISIL
1120
TTGEGEGRVG
1130
IILTLAMNIM
1140
STLQWAVNSS
1150
IDVDSLMRSV
1160

SRVFKFIDMP
1170
TEGIWPSGGQ
1209
MTVKDLTAKY
1219
TEGGNAILEN
1229
ISFSISPGQR
1239

VGLLGRTGSG
1249
KSTLLSAFLR
1259
LLNTEGEIQI
1269
DGVSWDSITL
1279
QQWRKAFGVI
1289

PQKVFIFSGT
1299
FRKNLDPYEQ
1309
WSDQEIWKVA
1319
DEVGLRSVIE
1329
QFPGKLDFVL
1339

VDGGCVLSHG
1349
HKQLMCLARS
1359
VLSKAKILLL
1369
DQPSAHLDPV
1379
TYQIIRRTLK
1389

QAFADCTVIL
1399
CEHRIEAMLE
1409
CQQFLVIEEN
1419
KVRQYDSIQK
1429
LLNERSLFRQ
1439

AISPSDRVKL
1449
FP
Residue
Distance (Å)
TRP401
3.479
VAL440
4.032
SER459
3.748
THR460
3.577
GLY461
3.066
ALA462
3.311
GLY463
3.186
LYS464
2.844
THR465
2.655
SER466
3.184
GLN493
3.281
PHE533
3.996
ILE546
3.966
THR547
3.220
LEU548
4.126
SER549
2.744
GLY550
3.889
GLY551
2.815
GLN552
2.946
TYR577
4.279
ASN965
4.475
TYR1219
3.493
Residue
Distance (Å)
ILE1226
3.842
ARG1245
3.762
THR1246
3.498
GLY1247
2.971
SER1248
3.511
GLY1249
3.289
LYS1250
2.726
SER1251
2.702
THR1252
3.085
GLN1291
3.155
GLN1330
3.665
PHE1331
4.816
CYS1344
3.531
VAL1345
3.034
LEU1346
4.070
SER1347
3.078
HIS1348
3.333
GLY1349
2.761
HIS1350
4.023
HIS1375
4.796
HIS1402
3.375
PDB ID: 8EIQ      The complex of phosphorylated human delta F508 cystic fibrosis transmembrane conductance regulator (CFTR) with Trikafta [elexacaftor (VX-445), tezacaftor (VX-661), ivacaftor (VX-770)] and ATP/Mg
Method Electron microscopy Resolution 3.00 Å Mutation Yes [2]
PDB Sequence
MQRSPLEKAS
10
VVSKLFFSWT
20
RPILRKGYRQ
30
RLELSDIYQI
40
PSVDSADNLS
50

EKLEREWDRE
60
LASKKNPKLI
70
NALRRCFFWR
80
FMFYGIFLYL
90
GEVTKAVQPL
100

LLGRIIASYD
110
PDNKEERSIA
120
IYLGIGLCLL
130
FIVRTLLLHP
140
AIFGLHHIGM
150

QMRIAMFSLI
160
YKKTLKLSSR
170
VLDKISIGQL
180
VSLLSNNLNK
190
FDEGLALAHF
200

VWIAPLQVAL
210
LMGLIWELLQ
220
ASAFCGLGFL
230
IVLALFQAGL
240
GRMMMKYRDQ
250

RAGKISERLV
260
ITSEMIENIQ
270
SVKAYCWEEA
280
MEKMIENLRQ
290
TELKLTRKAA
300

YVRYFNSSAF
310
FFSGFFVVFL
320
SVLPYALIKG
330
IILRKIFTTI
340
SFCIVLRMAV
350

TRQFPWAVQT
360
WYDSLGAINK
370
IQDFLQKQEY
380
KTLEYNLTTT
390
EVVMENVTAF
400

WEGTPVLKDI
444
NFKIERGQLL
454
AVAGSTGAGK
464
TSLLMVIMGE
474
LEPSEGKIKH
484

SGRISFCSQF
494
SWIMPGTIKE
504
NIIGVSYDEY
515
RYRSVIKACQ
525
LEEDISKFAE
535

KDNIVLGEGG
545
ITLSGGQRAR
555
ISLARAVYKD
565
ADLYLLDSPF
575
GYLDVLTEKE
585

IFESCVCKLM
595
ANKTRILVTS
605
KMEHLKKADK
615
ILILHEGSSY
625
FYGTFSELQN
635

LWNTYLRYIT
854
VHKSLIFVLI
864
WCLVIFLAEV
874
AASLVVLWLL
884
GSYAVIITST
910

SSYYVFYIYV
920
GVADTLLAMG
930
FFRGLPLVHT
940
LITVSKILHH
950
KMLHSVLQAP
960

MSTLNTLKAG
970
GILNRFSKDI
980
AILDDLLPLT
990
IFDFIQLLLI
1000
VIGAIAVVAV
1010

LQPYIFVATV
1020
PVIVAFIMLR
1030
AYFLQTSQQL
1040
KQLESEGRSP
1050
IFTHLVTSLK
1060

GLWTLRAFGR
1070
QPYFETLFHK
1080
ALNLHTANWF
1090
LYLSTLRWFQ
1100
MRIEMIFVIF
1110

FIAVTFISIL
1120
TTGEGEGRVG
1130
IILTLAMNIM
1140
STLQWAVNSS
1150
IDVDSLMRSV
1160

SRVFKFIDMP
1170
TEGIWPSGGQ
1209
MTVKDLTAKY
1219
TEGGNAILEN
1229
ISFSISPGQR
1239

VGLLGRTGSG
1249
KSTLLSAFLR
1259
LLNTEGEIQI
1269
DGVSWDSITL
1279
QQWRKAFGVI
1289

PQKVFIFSGT
1299
FRKNLDPYEQ
1309
WSDQEIWKVA
1319
DEVGLRSVIE
1329
QFPGKLDFVL
1339

VDGGCVLSHG
1349
HKQLMCLARS
1359
VLSKAKILLL
1369
DQPSAHLDPV
1379
TYQIIRRTLK
1389

QAFADCTVIL
1399
CEHRIEAMLE
1409
CQQFLVIEEN
1419
KVRQYDSIQK
1429
LLNERSLFRQ
1439

AISPSDRVKL
1449
FP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:401 or .A:440 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:493 or .A:533 or .A:546 or .A:547 or .A:548 or .A:549 or .A:550 or .A:551 or .A:552 or .A:577 or .A:1219 or .A:1226 or .A:1245 or .A:1246 or .A:1247 or .A:1248 or .A:1249 or .A:1250 or .A:1251 or .A:1252 or .A:1291 or .A:1330 or .A:1344 or .A:1345 or .A:1346 or .A:1347 or .A:1348 or .A:1349 or .A:1350 or .A:1375 or .A:1402; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TRP401
3.595
VAL440
4.392
SER459
4.445
THR460
3.725
GLY461
3.104
ALA462
3.691
GLY463
3.090
LYS464
2.523
THR465
2.655
SER466
3.184
GLN493
3.040
PHE533
3.988
ILE546
4.297
THR547
3.300
LEU548
4.120
SER549
2.429
GLY550
3.537
GLY551
2.662
GLN552
3.029
TYR577
4.350
TYR1219
3.529
Residue
Distance (Å)
ILE1226
4.241
ARG1245
4.119
THR1246
3.112
GLY1247
3.036
SER1248
3.724
GLY1249
3.252
LYS1250
2.602
SER1251
2.663
THR1252
3.045
GLN1291
3.183
GLN1330
3.711
CYS1344
3.703
VAL1345
2.907
LEU1346
4.160
SER1347
3.346
HIS1348
3.266
GLY1349
2.842
HIS1350
4.253
HIS1375
4.442
HIS1402
3.502
PDB ID: 8EIG      The complex of phosphorylated human delta F508 cystic fibrosis transmembrane conductance regulator (CFTR) with elexacaftor (VX-445) and ATP/Mg
Method Electron microscopy Resolution 3.60 Å Mutation Yes [2]
PDB Sequence
RSPLEKASVV
12
SKLFFSWTRP
22
ILRKGYRQRL
32
ELSDIYQIPS
42
VDSADNLSEK
52

LEREWDRELA
62
SKKNPKLINA
72
LRRCFFWRFM
82
FYGIFLYLGE
92
VTKAVQPLLL
102

GRIIASYDPD
112
NKEERSIAIY
122
LGIGLCLLFI
132
VRTLLLHPAI
142
FGLHHIGMQM
152

RIAMFSLIYK
162
KTLKLSSRVL
172
DKISIGQLVS
182
LLSNNLNKFD
192
EGLALAHFVW
202

IAPLQVALLM
212
GLIWELLQAS
222
AFCGLGFLIV
232
LALFQAGLGR
242
MMMKYRDQRA
252

GKISERLVIT
262
SEMIENIQSV
272
KAYCWEEAME
282
KMIENLRQTE
292
LKLTRKAAYV
302

RYFNSSAFFF
312
SGFFVVFLSV
322
LPYALIKGII
332
LRKIFTTISF
342
CIVLRMAVTR
352

QFPWAVQTWY
362
DSLGAINKIQ
372
DFLQKQEYKT
382
LEYNLTTTEV
392
VMENVTAFWE
402

GTPVLKDINF
446
KIERGQLLAV
456
AGSTGAGKTS
466
LLMVIMGELE
476
PSEGKIKHSG
486

RISFCSQFSW
496
IMPGTIKENI
506
IGVSYDEYRY
517
RSVIKACQLE
527
EDISKFAEKD
537

NIVLGEGGIT
547
LSGGQRARIS
557
LARAVYKDAD
567
LYLLDSPFGY
577
LDVLTEKEIF
587

ESCVCKLMAN
597
KTRILVTSKM
607
EHLKKADKIL
617
ILHEGSSYFY
627
GTFSELQNLW
846

NTYLRYITVH
856
KSLIFVLIWC
866
LVIFLAEVAA
876
SLVVLWLLGN
886
TPSYAVIITS
909

TSSYYVFYIY
919
VGVADTLLAM
929
GFFRGLPLVH
939
TLITVSKILH
949
HKMLHSVLQA
959

PMSTLNTLKA
969
GGILNRFSKD
979
IAILDDLLPL
989
TIFDFIQLLL
999
IVIGAIAVVA
1009

VLQPYIFVAT
1019
VPVIVAFIML
1029
RAYFLQTSQQ
1039
LKQLESEGRS
1049
PIFTHLVTSL
1059

KGLWTLRAFG
1069
RQPYFETLFH
1079
KALNLHTANW
1089
FLYLSTLRWF
1099
QMRIEMIFVI
1109

FFIAVTFISI
1119
LTTGEGEGRV
1129
GIILTLAMNI
1139
MSTLQWAVNS
1149
SIDVDSLMRS
1159

VSRVFKFIDM
1169
PTEGIWPSGG
1208
QMTVKDLTAK
1218
YTEGGNAILE
1228
NISFSISPGQ
1238

RVGLLGRTGS
1248
GKSTLLSAFL
1258
RLLNTEGEIQ
1268
IDGVSWDSIT
1278
LQQWRKAFGV
1288

IPQKVFIFSG
1298
TFRKNLDPYE
1308
QWSDQEIWKV
1318
ADEVGLRSVI
1328
EQFPGKLDFV
1338

LVDGGCVLSH
1348
GHKQLMCLAR
1358
SVLSKAKILL
1368
LDQPSAHLDP
1378
VTYQIIRRTL
1388

KQAFADCTVI
1398
LCEHRIEAML
1408
ECQQFLVIEE
1418
NKVRQYDSIQ
1428
K
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:173 or .A:401 or .A:440 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:493 or .A:532 or .A:533 or .A:546 or .A:547 or .A:548 or .A:549 or .A:550 or .A:551 or .A:552 or .A:577 or .A:965 or .A:1219 or .A:1220 or .A:1226 or .A:1245 or .A:1246 or .A:1247 or .A:1248 or .A:1249 or .A:1250 or .A:1251 or .A:1252 or .A:1291 or .A:1375 or .A:1402; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP173
3.256
TRP401
3.622
VAL440
3.975
SER459
3.439
THR460
3.507
GLY461
3.373
ALA462
3.100
GLY463
3.066
LYS464
3.123
THR465
2.816
SER466
3.549
GLN493
3.571
LYS532
4.853
PHE533
3.846
ILE546
3.813
THR547
3.246
LEU548
4.315
SER549
2.487
GLY550
3.813
Residue
Distance (Å)
GLY551
2.731
GLN552
3.553
TYR577
4.590
ASN965
4.186
TYR1219
3.523
THR1220
4.897
ILE1226
4.122
ARG1245
3.661
THR1246
2.650
GLY1247
3.272
SER1248
3.807
GLY1249
3.719
LYS1250
2.954
SER1251
2.682
THR1252
3.323
GLN1291
4.186
HIS1375
4.498
HIS1402
3.654
PDB ID: 6MSM      Phosphorylated, ATP-bound human cystic fibrosis transmembrane conductance regulator (CFTR)
Method Electron microscopy Resolution 3.20 Å Mutation Yes [3]
PDB Sequence
MQRSPLEKAS
10
VVSKLFFSWT
20
RPILRKGYRQ
30
RLELSDIYQI
40
PSVDSADNLS
50

EKLEREWDRE
60
LASKKNPKLI
70
NALRRCFFWR
80
FMFYGIFLYL
90
GEVTKAVQPL
100

LLGRIIASYD
110
PDNKEERSIA
120
IYLGIGLCLL
130
FIVRTLLLHP
140
AIFGLHHIGM
150

QMRIAMFSLI
160
YKKTLKLSSR
170
VLDKISIGQL
180
VSLLSNNLNK
190
FDEGLALAHF
200

VWIAPLQVAL
210
LMGLIWELLQ
220
ASAFCGLGFL
230
IVLALFQAGL
240
GRMMMKYRDQ
250

RAGKISERLV
260
ITSEMIENIQ
270
SVKAYCWEEA
280
MEKMIENLRQ
290
TELKLTRKAA
300

YVRYFNSSAF
310
FFSGFFVVFL
320
SVLPYALIKG
330
IILRKIFTTI
340
SFCIVLRMAV
350

TRQFPWAVQT
360
WYDSLGAINK
370
IQDFLQKQEY
380
KTLEYNLTTT
390
EVVMENVTAF
400

WEEGFGELFL
435
LGTPVLKDIN
445
FKIERGQLLA
455
VAGSTGAGKT
465
SLLMVIMGEL
475

EPSEGKIKHS
485
GRISFCSQFS
495
WIMPGTIKEN
505
IIFGVSYDEY
515
RYRSVIKACQ
525

LEEDISKFAE
535
KDNIVLGEGG
545
ITLSGGQRAR
555
ISLARAVYKD
565
ADLYLLDSPF
575

GYLDVLTEKE
585
IFESCVCKLM
595
ANKTRILVTS
605
KMEHLKKADK
615
ILILHEGSSY
625

FYGTFSELQN
635
LQTWNTYLRY
852
ITVHKSLIFV
862
LIWCLVIFLA
872
EVAASLVVLW
882

LLGNTPLNNS
902
YAVIITSTSS
912
YYVFYIYVGV
922
ADTLLAMGFF
932
RGLPLVHTLI
942

TVSKILHHKM
952
LHSVLQAPMS
962
TLNTLKAGGI
972
LNRFSKDIAI
982
LDDLLPLTIF
992

DFIQLLLIVI
1002
GAIAVVAVLQ
1012
PYIFVATVPV
1022
IVAFIMLRAY
1032
FLQTSQQLKQ
1042

LESEGRSPIF
1052
THLVTSLKGL
1062
WTLRAFGRQP
1072
YFETLFHKAL
1082
NLHTANWFLY
1092

LSTLRWFQMR
1102
IEMIFVIFFI
1112
AVTFISILTT
1122
GEGEGRVGII
1132
LTLAMNIMST
1142

LQWAVNSSID
1152
VDSLMRSVSR
1162
VFKFIDMPTE
1172
GDIWPSGGQM
1210
TVKDLTAKYT
1220

EGGNAILENI
1230
SFSISPGQRV
1240
GLLGRTGSGK
1250
STLLSAFLRL
1260
LNTEGEIQID
1270

GVSWDSITLQ
1280
QWRKAFGVIP
1290
QKVFIFSGTF
1300
RKNLDPYEQW
1310
SDQEIWKVAD
1320

EVGLRSVIEQ
1330
FPGKLDFVLV
1340
DGGCVLSHGH
1350
KQLMCLARSV
1360
LSKAKILLLD
1370

QPSAHLDPVT
1380
YQIIRRTLKQ
1390
AFADCTVILC
1400
EHRIEAMLEC
1410
QQFLVIEENK
1420

VRQYDSIQKL
1430
LNERSLFRQA
1440
ISPSDRVKLF
1450
P
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:173 or .A:401 or .A:440 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:493 or .A:529 or .A:532 or .A:533 or .A:546 or .A:547 or .A:548 or .A:549 or .A:550 or .A:551 or .A:552 or .A:577 or .A:965 or .A:1219 or .A:1226 or .A:1245 or .A:1246 or .A:1247 or .A:1248 or .A:1249 or .A:1250 or .A:1251 or .A:1252 or .A:1291 or .A:1330 or .A:1331 or .A:1344 or .A:1345 or .A:1346 or .A:1347 or .A:1348 or .A:1349 or .A:1350 or .A:1371 or .A:1375 or .A:1402; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP173
4.491
TRP401
3.436
VAL440
3.302
SER459
3.984
THR460
3.546
GLY461
3.485
ALA462
3.644
GLY463
3.369
LYS464
2.695
THR465
2.627
SER466
2.867
GLN493
3.009
ASP529
4.740
LYS532
4.940
PHE533
3.326
ILE546
3.717
THR547
3.117
LEU548
4.866
SER549
2.893
GLY550
4.132
GLY551
2.972
GLN552
2.633
TYR577
4.126
ASN965
4.006
Residue
Distance (Å)
TYR1219
3.253
ILE1226
3.994
ARG1245
4.453
THR1246
2.780
GLY1247
3.387
SER1248
4.088
GLY1249
3.042
LYS1250
2.507
SER1251
2.639
THR1252
2.890
GLN1291
2.718
GLN1330
4.201
PHE1331
4.547
CYS1344
3.683
VAL1345
3.197
LEU1346
4.419
SER1347
3.424
HIS1348
3.683
GLY1349
2.752
HIS1350
4.031
GLN1371
4.646
HIS1375
4.513
HIS1402
3.858
PDB ID: 6O1V      Complex of human cystic fibrosis transmembrane conductance regulator (CFTR) and GLPG1837
Method Electron microscopy Resolution 3.20 Å Mutation Yes [4]
PDB Sequence
MQRSPLEKAS
10
VVSKLFFSWT
20
RPILRKGYRQ
30
RLELSDIYQI
40
PSVDSADNLS
50

EKLEREWDRE
60
LASKKNPKLI
70
NALRRCFFWR
80
FMFYGIFLYL
90
GEVTKAVQPL
100

LLGRIIASYD
110
PDNKEERSIA
120
IYLGIGLCLL
130
FIVRTLLLHP
140
AIFGLHHIGM
150

QMRIAMFSLI
160
YKKTLKLSSR
170
VLDKISIGQL
180
VSLLSNNLNK
190
FDEGLALAHF
200

VWIAPLQVAL
210
LMGLIWELLQ
220
ASAFCGLGFL
230
IVLALFQAGL
240
GRMMMKYRDQ
250

RAGKISERLV
260
ITSEMIENIQ
270
SVKAYCWEEA
280
MEKMIENLRQ
290
TELKLTRKAA
300

YVRYFNSSAF
310
FFSGFFVVFL
320
SVLPYALIKG
330
IILRKIFTTI
340
SFCIVLRMAV
350

TRQFPWAVQT
360
WYDSLGAINK
370
IQDFLQKQEY
380
KTLEYNLTTT
390
EVVMENVTAF
400

WEEGFGELFG
437
TPVLKDINFK
447
IERGQLLAVA
457
GSTGAGKTSL
467
LMVIMGELEP
477

SEGKIKHSGR
487
ISFCSQFSWI
497
MPGTIKENII
507
FGVSYDEYRY
517
RSVIKACQLE
527

EDISKFAEKD
537
NIVLGEGGIT
547
LSGGQRARIS
557
LARAVYKDAD
567
LYLLDSPFGY
577

LDVLTEKEIF
587
ESCVCKLMAN
597
KTRILVTSKM
607
EHLKKADKIL
617
ILHEGSSYFY
627

GTFSELQNLQ
637
TWNTYLRYIT
854
VHKSLIFVLI
864
WCLVIFLAEV
874
AASLVVLWLL
884

GNTPLNNSYA
904
VIITSTSSYY
914
VFYIYVGVAD
924
TLLAMGFFRG
934
LPLVHTLITV
944

SKILHHKMLH
954
SVLQAPMSTL
964
NTLKAGGILN
974
RFSKDIAILD
984
DLLPLTIFDF
994

IQLLLIVIGA
1004
IAVVAVLQPY
1014
IFVATVPVIV
1024
AFIMLRAYFL
1034
QTSQQLKQLE
1044

SEGRSPIFTH
1054
LVTSLKGLWT
1064
LRAFGRQPYF
1074
ETLFHKALNL
1084
HTANWFLYLS
1094

TLRWFQMRIE
1104
MIFVIFFIAV
1114
TFISILTTGE
1124
GEGRVGIILT
1134
LAMNIMSTLQ
1144

WAVNSSIDVD
1154
SLMRSVSRVF
1164
KFIDMPTEGD
1202
IWPSGGQMTV
1212
KDLTAKYTEG
1222

GNAILENISF
1232
SISPGQRVGL
1242
LGRTGSGKST
1252
LLSAFLRLLN
1262
TEGEIQIDGV
1272

SWDSITLQQW
1282
RKAFGVIPQK
1292
VFIFSGTFRK
1302
NLDPYEQWSD
1312
QEIWKVADEV
1322

GLRSVIEQFP
1332
GKLDFVLVDG
1342
GCVLSHGHKQ
1352
LMCLARSVLS
1362
KAKILLLDQP
1372

SAHLDPVTYQ
1382
IIRRTLKQAF
1392
ADCTVILCEH
1402
RIEAMLECQQ
1412
FLVIEENKVR
1422

QYDSIQKLLN
1432
ERSLFRQAIS
1442
PSDRVKLFP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:173 or .A:401 or .A:440 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:493 or .A:529 or .A:532 or .A:533 or .A:546 or .A:547 or .A:548 or .A:549 or .A:550 or .A:551 or .A:552 or .A:577 or .A:965 or .A:1219 or .A:1226 or .A:1245 or .A:1246 or .A:1247 or .A:1248 or .A:1249 or .A:1250 or .A:1251 or .A:1252 or .A:1291 or .A:1330 or .A:1331 or .A:1344 or .A:1345 or .A:1346 or .A:1347 or .A:1348 or .A:1349 or .A:1350 or .A:1371 or .A:1375 or .A:1402; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP173
4.436
TRP401
3.410
VAL440
3.354
SER459
3.960
THR460
3.468
GLY461
3.596
ALA462
3.385
GLY463
3.316
LYS464
2.814
THR465
2.643
SER466
2.746
GLN493
2.935
ASP529
4.736
LYS532
4.991
PHE533
3.256
ILE546
3.568
THR547
3.080
LEU548
4.818
SER549
2.915
GLY550
3.900
GLY551
2.815
GLN552
2.658
TYR577
4.172
ASN965
4.109
Residue
Distance (Å)
TYR1219
3.324
ILE1226
3.971
ARG1245
4.563
THR1246
3.164
GLY1247
3.388
SER1248
3.777
GLY1249
3.068
LYS1250
2.623
SER1251
2.543
THR1252
2.801
GLN1291
2.726
GLN1330
3.978
PHE1331
4.438
CYS1344
3.634
VAL1345
3.248
LEU1346
4.518
SER1347
3.551
HIS1348
3.372
GLY1349
2.678
HIS1350
4.133
GLN1371
4.706
HIS1375
4.581
HIS1402
3.723
PDB ID: 6O2P      Complex of ivacaftor with cystic fibrosis transmembrane conductance regulator (CFTR)
Method Electron microscopy Resolution 3.30 Å Mutation Yes [4]
PDB Sequence
MQRSPLEKAS
10
VVSKLFFSWT
20
RPILRKGYRQ
30
RLELSDIYQI
40
PSVDSADNLS
50

EKLEREWDRE
60
LASKKNPKLI
70
NALRRCFFWR
80
FMFYGIFLYL
90
GEVTKAVQPL
100

LLGRIIASYD
110
PDNKEERSIA
120
IYLGIGLCLL
130
FIVRTLLLHP
140
AIFGLHHIGM
150

QMRIAMFSLI
160
YKKTLKLSSR
170
VLDKISIGQL
180
VSLLSNNLNK
190
FDEGLALAHF
200

VWIAPLQVAL
210
LMGLIWELLQ
220
ASAFCGLGFL
230
IVLALFQAGL
240
GRMMMKYRDQ
250

RAGKISERLV
260
ITSEMIENIQ
270
SVKAYCWEEA
280
MEKMIENLRQ
290
TELKLTRKAA
300

YVRYFNSSAF
310
FFSGFFVVFL
320
SVLPYALIKG
330
IILRKIFTTI
340
SFCIVLRMAV
350

TRQFPWAVQT
360
WYDSLGAINK
370
IQDFLQKQEY
380
KTLEYNLTTT
390
EVVMENVTAF
400

WEEGFGELFG
437
TPVLKDINFK
447
IERGQLLAVA
457
GSTGAGKTSL
467
LMVIMGELEP
477

SEGKIKHSGR
487
ISFCSQFSWI
497
MPGTIKENII
507
FGVSYDEYRY
517
RSVIKACQLE
527

EDISKFAEKD
537
NIVLGEGGIT
547
LSGGQRARIS
557
LARAVYKDAD
567
LYLLDSPFGY
577

LDVLTEKEIF
587
ESCVCKLMAN
597
KTRILVTSKM
607
EHLKKADKIL
617
ILHEGSSYFY
627

GTFSELQNLQ
637
TWNTYLRYIT
854
VHKSLIFVLI
864
WCLVIFLAEV
874
AASLVVLWLL
884

GNTPLNNSYA
904
VIITSTSSYY
914
VFYIYVGVAD
924
TLLAMGFFRG
934
LPLVHTLITV
944

SKILHHKMLH
954
SVLQAPMSTL
964
NTLKAGGILN
974
RFSKDIAILD
984
DLLPLTIFDF
994

IQLLLIVIGA
1004
IAVVAVLQPY
1014
IFVATVPVIV
1024
AFIMLRAYFL
1034
QTSQQLKQLE
1044

SEGRSPIFTH
1054
LVTSLKGLWT
1064
LRAFGRQPYF
1074
ETLFHKALNL
1084
HTANWFLYLS
1094

TLRWFQMRIE
1104
MIFVIFFIAV
1114
TFISILTTGE
1124
GEGRVGIILT
1134
LAMNIMSTLQ
1144

WAVNSSIDVD
1154
SLMRSVSRVF
1164
KFIDMPTEGD
1202
IWPSGGQMTV
1212
KDLTAKYTEG
1222

GNAILENISF
1232
SISPGQRVGL
1242
LGRTGSGKST
1252
LLSAFLRLLN
1262
TEGEIQIDGV
1272

SWDSITLQQW
1282
RKAFGVIPQK
1292
VFIFSGTFRK
1302
NLDPYEQWSD
1312
QEIWKVADEV
1322

GLRSVIEQFP
1332
GKLDFVLVDG
1342
GCVLSHGHKQ
1352
LMCLARSVLS
1362
KAKILLLDQP
1372

SAHLDPVTYQ
1382
IIRRTLKQAF
1392
ADCTVILCEH
1402
RIEAMLECQQ
1412
FLVIEENKVR
1422

QYDSIQKLLN
1432
ERSLFRQAIS
1442
PSDRVKLFP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:173 or .A:401 or .A:440 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:493 or .A:529 or .A:532 or .A:533 or .A:546 or .A:547 or .A:548 or .A:549 or .A:550 or .A:551 or .A:552 or .A:577 or .A:965 or .A:1219 or .A:1226 or .A:1245 or .A:1246 or .A:1247 or .A:1248 or .A:1249 or .A:1250 or .A:1251 or .A:1252 or .A:1291 or .A:1330 or .A:1331 or .A:1344 or .A:1345 or .A:1346 or .A:1347 or .A:1348 or .A:1349 or .A:1350 or .A:1370 or .A:1371 or .A:1375 or .A:1402; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP173
4.451
TRP401
3.507
VAL440
3.283
SER459
3.917
THR460
3.509
GLY461
3.340
ALA462
3.116
GLY463
3.133
LYS464
2.767
THR465
2.725
SER466
2.732
GLN493
2.841
ASP529
4.882
LYS532
4.981
PHE533
3.278
ILE546
3.495
THR547
3.051
LEU548
4.449
SER549
3.164
GLY550
3.182
GLY551
2.756
GLN552
2.702
TYR577
3.932
ASN965
3.990
Residue
Distance (Å)
TYR1219
3.286
ILE1226
3.985
ARG1245
4.108
THR1246
3.279
GLY1247
3.406
SER1248
3.367
GLY1249
3.268
LYS1250
2.748
SER1251
2.727
THR1252
2.598
GLN1291
2.859
GLN1330
3.599
PHE1331
4.695
CYS1344
3.716
VAL1345
2.867
LEU1346
3.912
SER1347
3.509
HIS1348
3.420
GLY1349
2.676
HIS1350
4.399
ASP1370
4.797
GLN1371
4.480
HIS1375
4.437
HIS1402
3.496
PDB ID: 1XMI      Crystal structure of human F508A NBD1 domain with ATP
Method X-ray diffraction Resolution 2.25 Å Mutation Yes [5]
PDB Sequence
STTEVVMENV
397
TAFWEEGFGE
407
LFEKSFSNFS
434
LLGTPVLKDI
444
NFKIERGQLL
454

AVAGSTGAGK
464
TSLLMMIMGE
474
LEPSEGKIKH
484
SGRISFCSQF
494
SWIMPGTIKE
504

NIIAGVSYDE
514
YRYRSVIKAC
524
QLEEDISKFA
534
EKDNIVLGEG
544
GITLSGGQRA
554

RISLARAVYK
564
DADLYLLDSP
574
FGYLDVLTEK
584
EIFESCVCKL
594
MANKTRILVT
604

SKMEHLKKAD
614
KILILHEGSS
624
YFYGTFSELQ
634
NLQPDFSSKL
644
MGCDSFDQFS
654

AERRNSILTE
664
TLRRFSL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:401 or .A:440 or .A:458 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:493; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TRP401
3.193
VAL440
3.353
GLY458
4.859
SER459
3.955
THR460
3.156
GLY461
3.013
Residue
Distance (Å)
ALA462
3.451
GLY463
3.189
LYS464
2.841
THR465
2.895
SER466
2.682
GLN493
3.036
PDB ID: 2BBO      Human NBD1 with Phe508
Method X-ray diffraction Resolution 2.55 Å Mutation Yes [6]
PDB Sequence
TTEVVMENVT
398
AFWEEGLGTP
439
VLKDINFKIE
449
RGQLLAVAGS
459
TGAGKTSLLM
469

MIMGELEPSE
479
GKIKHSGRIS
489
FCSQFSWIMP
499
GTIKENIIFG
509
VSYDEYRYRS
519

VIKACQLEED
529
ISKFAEKDNI
539
VLGEGGITLS
549
EGQQAKISLA
559
RAVYKDADLY
569

LLDSPFGYLD
579
VLTEKEIFES
589
CVCKLMANKT
599
RILVTSKMEH
609
LKKADKILIL
619

HEGSSYFYGT
629
FSELQNLQPD
639
FSSKLMSFDQ
652
FSAERRNSIL
662
TETLRRFSLE
672

GDAP
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:401 or .A:403 or .A:404 or .A:440 or .A:458 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:493 or .A:577; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TRP401
3.267
GLU403
4.136
GLY404
4.346
VAL440
3.664
GLY458
4.910
SER459
3.860
THR460
3.162
GLY461
2.819
Residue
Distance (Å)
ALA462
3.281
GLY463
2.913
LYS464
2.741
THR465
2.757
SER466
2.841
GLN493
2.943
TYR577
2.949
PDB ID: 2BBS      Human deltaF508 NBD1 with three solubilizing mutations
Method X-ray diffraction Resolution 2.05 Å Mutation Yes [6]
PDB Sequence
STTEVVMENV
397
TAFWEEGFGE
407
LFEKAKGTPV
440
LKDINFKIER
450
GQLLAVAGST
460

GAGKTSLLMM
470
IMGELEPSEG
480
KIKHSGRISF
490
CSQNSWIMPG
500
TIKENIIGVS
511

YDEYRYRSVI
521
KACQLEEDIS
531
KFAEKDNIVL
541
ITLSGGQRAR
555
ISLARAVYKD
565

ADLYLLDSPF
575
GYLDVLTEKE
585
IFESCVCKLM
595
ANKTRILVTS
605
KMEHLKKADK
615

ILILHEGSSY
625
FYGTFSELQN
635
LRPDFSSKLM
645
SFDQFSAERR
658
NSILTETLHR
668

FSL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:401 or .A:440 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:493 or .A:659; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TRP401
3.291
VAL440
3.450
SER459
3.893
THR460
3.515
GLY461
3.032
ALA462
3.140
Residue
Distance (Å)
GLY463
3.034
LYS464
2.743
THR465
2.867
SER466
2.656
GLN493
3.044
ASN659
4.824
PDB ID: 4WZ6      Human CFTR aa389-678 (NBD1), deltaF508 with three solubilizing mutations, bound ATP
Method X-ray diffraction Resolution 2.05 Å Mutation Yes [7]
PDB Sequence
TTEVVMENVT
398
AFWEEGFGEL
408
FEKAKQSLLG
437
TPVLKDINFK
447
IERGQLLAVA
457

GSTGAGKTSL
467
LMMIMGELEP
477
SEGKIKHSGR
487
ISFCSQNSWI
497
MPGTIKENII
507

GVSYDEYRYR
517
SVIKACQLEE
527
DISKFAEKDN
537
IVLGITLSGG
550
QRARISLARA
560

VYKDADLYLL
570
DSPFGYLDVL
580
TEKEIFESCV
590
CKLMANKTRI
600
LVTSKMEHLK
610

KADKILILHE
620
GSSYFYGTFS
630
ELQNLRPDFS
640
SKLMSFDQFS
653
AERRNSILTE
663

TLHRFSLE
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:401 or .A:440 or .A:458 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:469 or .A:493; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TRP401
3.118
VAL440
3.591
GLY458
4.886
SER459
3.616
THR460
2.881
GLY461
2.946
ALA462
3.136
Residue
Distance (Å)
GLY463
3.233
LYS464
2.631
THR465
2.844
SER466
2.633
MET469
3.455
GLN493
2.830
PDB ID: 1XMJ      Crystal structure of human deltaF508 human NBD1 domain with ATP
Method X-ray diffraction Resolution 2.30 Å Mutation Yes [5]
PDB Sequence
EVVMENVTAF
400
WETPVLKDIN
445
FKIERGQLLA
455
VAGSTGAGKT
465
SLLMMIMGEL
475

EPSEGKIKHS
485
GRISFCSQFS
495
WIMPGTIKEN
505
IIGVSYDEYR
516
YRSVIKACQL
526

EEDISKFAEK
536
DNIVLGEGGI
546
TLSEGQQAKI
556
SLARAVYKDA
566
DLYLLDSPFG
576

YLDVLTEKEI
586
FESCVCKLMA
596
NKTRILVTSK
606
MEHLKKADKI
616
LILHEGSSYF
626

YGTFSELQNL
636
QPDFSSKLMS
649
FDQFSAERRN
659
SILTETLRRF
669
SLEGDA
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:401 or .A:402 or .A:440 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:493; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TRP401
3.300
GLU402
4.929
VAL440
3.559
SER459
3.723
THR460
3.217
GLY461
3.142
Residue
Distance (Å)
ALA462
3.168
GLY463
3.385
LYS464
2.670
THR465
2.820
SER466
2.644
GLN493
3.388
PDB ID: 2BBT      Human deltaF508 NBD1 with two solublizing mutations.
Method X-ray diffraction Resolution 2.30 Å Mutation Yes [6]
PDB Sequence
TEVVMENVTA
399
FWEEGFGELF
409
EKAKGTPVLK
442
DINFKIERGQ
452
LLAVAGSTGA
462

GKTSLLMMIM
472
GELEPSEGKI
482
KHSGRISFCS
492
QNSWIMPGTI
502
KENIIGVSYD
513

EYRYRSVIKA
523
CQLEEDISKF
533
AEKDNIVLGG
545
ITLSGGQRAR
555
ISLARAVYKD
565

ADLYLLDSPF
575
GYLDVLTEKE
585
IFESCVCKLM
595
ANKTRILVTS
605
KMEHLKKADK
615

ILILHEGSSY
625
FYGTFSELQN
635
LRPDFSSDSF
650
DQFSAERRNS
660
ILTETLHRF
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:401 or .A:440 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:493; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TRP401
3.395
VAL440
3.511
SER459
3.805
THR460
3.252
GLY461
3.121
ALA462
3.234
Residue
Distance (Å)
GLY463
3.311
LYS464
2.747
THR465
2.859
SER466
2.512
GLN493
3.302
PDB ID: 6GJQ      human NBD1 of CFTR in complex with nanobody T27
Method X-ray diffraction Resolution 2.49 Å Mutation Yes [8]
PDB Sequence
DINFKIERGQ
452
LLAVAGSTGA
462
GKTSLLMMIM
472
GELEPSRISF
490
CPQFSWIMPG
500

TIKENIIFGV
510
SYDEYRYRSV
520
IKACQLEEDI
530
SKFPEKDNTV
540
LGEGGITLSG
550

GQRARISLAR
560
AVYKDADLYL
570
LDSPFGYLDV
580
LTEKEIFESC
590
VCKLMANKTR
600

ILVTSKMEHL
610
KKADKILILH
620
EGSSYFYGTF
630
SELQNLQ
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:443 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:493 or .A:572 or .A:622; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ASP443
4.139
SER459
3.681
THR460
3.662
GLY461
3.118
ALA462
3.286
GLY463
3.047
Residue
Distance (Å)
LYS464
2.924
THR465
2.782
SER466
2.793
GLN493
2.830
ASP572
4.956
GLY622
4.588
PDB ID: 6ZE1      human NBD1 of CFTR in complex with nanobody G11a
Method X-ray diffraction Resolution 2.71 Å Mutation Yes [9]
PDB Sequence
NGDDSLFFSN
432
FSLLGTPVLK
442
DINFKIERGQ
452
LLAVAGSTGA
462
GKTSLLMMIM
472

GELEPSEGKI
482
KHSGRISFCP
492
QFSWIMPGTI
502
KENIIFGVSY
512
DEYRYRSVIK
522

ACQLEEDISK
532
FPEKDNTVLG
542
EGGITLSGGQ
552
RARISLARAV
562
YKDADLYLLD
572

SPFGYLDVLT
582
EKEIFESCVC
592
KLMANKTRIL
602
VTSKMEHLKK
612
ADKILILHEG
622

SSYFYGTFSE
632
LQNLQ
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:440 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:493 or .A:572 or .A:603; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
VAL440
3.604
SER459
3.838
THR460
2.405
GLY461
3.677
ALA462
3.933
GLY463
3.069
Residue
Distance (Å)
LYS464
2.879
THR465
2.565
SER466
2.583
GLN493
2.680
ASP572
3.588
VAL603
4.206
PDB ID: 2PZG      Minimal human CFTR first nucleotide binding domain as a monomer
Method X-ray diffraction Resolution 1.80 Å Mutation Yes [10]
PDB Sequence
TEVVMENVTA
399
FWEEGGTPVL
441
KDINFKIERG
451
QLLAVAGSTG
461
AGKTSLLMMI
471

MGELEPSEGK
481
IKHSGRISFC
491
SQFSWIMPGT
501
IKENIIFGVS
511
YDEYRYRSVI
521

KACQLEEDIS
531
KFAEKDNIVL
541
GEGGITLSGG
551
QRARISLARA
561
VYKDADLYLL
571

DSPFGYLDVL
581
TEKEIFESCV
591
CKLMANKTRI
601
LVTSKMEHLK
611
KADKILILHE
621

GSSYFYGTFS
631
ELQNPDFSSK
643
LMG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:401 or .A:440 or .A:458 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:469 or .A:493; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TRP401
3.051
VAL440
3.387
GLY458
4.977
SER459
3.858
THR460
2.741
GLY461
3.044
ALA462
3.330
Residue
Distance (Å)
GLY463
3.104
LYS464
2.809
THR465
2.849
SER466
2.688
MET469
4.250
GLN493
2.606
PDB ID: 2PZE      Minimal human CFTR first nucleotide binding domain as a head-to-tail dimer
Method X-ray diffraction Resolution 1.70 Å Mutation Yes [10]
PDB Sequence
SLTTTEVVME
395
NVTAFWEEGG
437
TPVLKDINFK
447
IERGQLLAVA
457
GSTGAGKTSL
467

LMMIMGELEP
477
SEGKIKHSGR
487
ISFCSQFSWI
497
MPGTIKENII
507
FGVSYDEYRY
517

RSVIKACQLE
527
EDISKFAEKD
537
NIVLGEGGIT
547
LSGGQRARIS
557
LARAVYKDAD
567

LYLLDSPFGY
577
LDVLTEKEIF
587
ESCVCKLMAN
597
KTRILVTSKM
607
EHLKKADKIL
617

ILHEGSSYFY
627
GTFSELQNLD
639
FSSKLM
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:401 or .A:440 or .A:458 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:493; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TRP401
3.395
VAL440
3.554
GLY458
4.991
SER459
3.968
THR460
2.666
GLY461
2.936
Residue
Distance (Å)
ALA462
3.254
GLY463
2.977
LYS464
2.789
THR465
2.861
SER466
2.735
GLN493
3.004
PDB ID: 5TF7      Nucleotide-binding domain 1 of the human cystic fibrosis transmembrane conductance regulator (CFTR) with ATP
Method X-ray diffraction Resolution 1.93 Å Mutation Yes [11]
PDB Sequence
TEVVMENVTA
399
FWEEGGTPVL
441
KDINFKIERG
451
QLLAVAGSTG
461
AGKTSLLMMI
471

MGELEPSEGK
481
IKHSGRISFC
491
SQFSWIMPGT
501
IKENIIFGVS
511
YDEYRYRSVI
521

KACQLEEDIS
531
KFAEKDNIVL
541
GEGGITLSGG
551
QRARISLARA
561
VYKDADLYLL
571

DSPFGYLDVL
581
TEKEIFESCV
591
CKLMANKTRI
601
LVTSKMEHLK
611
KADKILILHE
621

GSSYFYGTFS
631
ELQNLQ
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:401 or .A:440 or .A:458 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:469 or .A:493; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TRP401
3.305
VAL440
3.361
GLY458
4.908
SER459
3.892
THR460
2.673
GLY461
2.931
ALA462
3.381
Residue
Distance (Å)
GLY463
3.119
LYS464
2.552
THR465
2.814
SER466
2.604
MET469
4.880
GLN493
3.025
PDB ID: 6GJS      Human NBD1 of CFTR in complex with nanobodies D12 and T4
Method X-ray diffraction Resolution 1.95 Å Mutation No [8]
PDB Sequence
SLTTTEVVME
395
NVTAFWEEGG
437
TPVLKDINFK
447
IERGQLLAVA
457
GSTGAGKTSL
467

LMMIMGELEP
477
SEGKIKHSGR
487
ISFCSQFSWI
497
MPGTIKENII
507
FGVSYDEYRY
517

RSVIKACQLE
527
EDISKFAEKD
537
NIVLGEGGIT
547
LSGGQRARIS
557
LARAVYKDAD
567

LYLLDSPFGY
577
LDVLTEKEIF
587
ESCVCKLMAN
597
KTRILVTSKM
607
EHLKKADKIL
617

ILHEGSSYFY
627
GTFSELQNL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:401 or .A:440 or .A:458 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:469 or .A:493; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TRP401
3.185
VAL440
3.495
GLY458
4.842
SER459
3.992
THR460
2.778
GLY461
3.042
ALA462
3.300
Residue
Distance (Å)
GLY463
3.131
LYS464
2.714
THR465
2.916
SER466
2.698
MET469
4.957
GLN493
2.947
PDB ID: 6UK1      Crystal structure of nucleotide-binding domain 2 (NBD2) of the human Cystic Fibrosis Transmembrane Conductance Regulator (CFTR)
Method X-ray diffraction Resolution 2.69 Å Mutation Yes [12]
PDB Sequence
DIWPSGGQMT
1211
VKDLTAKYTE
1221
GGNAILENIS
1231
FSISPGQRVG
1241
LLGRTGSGKS
1251

TLLLAFLRLL
1261
NTEGEIQIDG
1271
VSWDSITLEQ
1281
WRKAFGVIPQ
1291
DVFIFSGTFR
1301

KNLDPNEQWS
1311
DQEIWKVADE
1321
VGLRSVIEQF
1331
PGGLDFVLVD
1341
GGCVLSHGHK
1351

QLMCLARAVL
1361
SKAKILLLDE
1371
PSAHLDPVTY
1381
QIIRRTLKQA
1391
FADCTVILCE
1401

ARIEAMLECD
1411
QFLVIEENKV
1421
RQYDSIQKL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:1219 or .A:1226 or .A:1245 or .A:1246 or .A:1247 or .A:1248 or .A:1249 or .A:1250 or .A:1251 or .A:1252 or .A:1371 or .A:1375; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TYR1219
3.370
ILE1226
3.288
ARG1245
3.773
THR1246
2.697
GLY1247
2.859
SER1248
3.651
Residue
Distance (Å)
GLY1249
3.180
LYS1250
2.733
SER1251
2.880
THR1252
2.584
GLU1371
3.500
HIS1375
4.931
PDB ID: 6GK4      Human NBD1 of CFTR in complex with nanobodies D12 and T8
Method X-ray diffraction Resolution 2.91 Å Mutation No [8]
PDB Sequence
TEVVMENVTA
399
FWPVLKDINF
446
KIERGQLLAV
456
AGSTGAGKTS
466
LLMMIMGELE
476

PSEGKIKHSG
486
RISFCSQFSW
496
IMPGTIKENI
506
IFGVSYDEYR
516
YRSVIKACQL
526

EEDISKFAEK
536
DNIVLGEGGI
546
TLSGGQRARI
556
SLARAVYKDA
566
DLYLLDSPFG
576

YLDVLTEKEI
586
FESCVCKLMA
596
NKTRILVTSK
606
MEHLKKADKI
616
LILHEGSSYF
626

YGTFSELQNL
636
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:401 or .A:440 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:493 or .A:572; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TRP401
3.476
VAL440
3.491
SER459
4.042
THR460
3.801
GLY461
3.175
ALA462
3.822
Residue
Distance (Å)
GLY463
3.362
LYS464
2.977
THR465
1.959
SER466
2.044
GLN493
2.934
ASP572
4.874
PDB ID: 6GKD      human NBD1 of CFTR in complex with nanobodies D12 and G3a
Method X-ray diffraction Resolution 2.99 Å Mutation No [8]
PDB Sequence
TTEVVMENVT
398
AFWEEGGTPV
440
LKDINFKIER
450
GQLLAVAGST
460
GAGKTSLLMM
470

IMGELEPSEG
480
KIKHSGRISF
490
CSQFSWIMPG
500
TIKENIIFGV
510
SYDEYRYRSV
520

IKACQLEEDI
530
SKFAEKDNIV
540
LGEGGITLSG
550
GQRARISLAR
560
AVYKDADLYL
570

LDSPFGYLDV
580
LTEKEIFESC
590
VCKLMANKTR
600
ILVTSKMEHL
610
KKADKILILH
620

EGSSYFYGTF
630
SELQNL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:401 or .A:440 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:469 or .A:493; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TRP401
3.310
VAL440
3.776
SER459
4.099
THR460
3.348
GLY461
3.218
ALA462
3.776
Residue
Distance (Å)
GLY463
3.341
LYS464
2.630
THR465
2.591
SER466
2.777
MET469
4.084
GLN493
2.567
PDB ID: 2PZF      Minimal human CFTR first nucleotide binding domain as a head-to-tail dimer with delta F508
Method X-ray diffraction Resolution 2.00 Å Mutation Yes [10]
PDB Sequence
SLTTTEVVME
395
NVTAFWGGTP
439
VLKDINFKIE
449
RGQLLAVAGS
459
TGAGKTSLLM
469

MIMGELEPSE
479
GKIKHSGRIS
489
FCSQFSWIMP
499
GTIKENIIGV
510
SYDEYRYRSV
520

IKACQLEEDI
530
SKFAEKDNIV
540
LGEGGITLSG
550
GQRARISLAR
560
AVYKDADLYL
570

LDSPFGYLDV
580
LTEKEIFESC
590
VCKLMANKTR
600
ILVTSKMEHL
610
KKADKILILH
620

EGSSYFYGTF
630
SELQNLDFSS
642
KLMG
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:401 or .A:440 or .A:458 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:493; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TRP401
3.416
VAL440
3.412
GLY458
4.903
SER459
3.945
THR460
2.593
GLY461
2.907
Residue
Distance (Å)
ALA462
3.187
GLY463
2.933
LYS464
2.746
THR465
2.933
SER466
2.591
GLN493
2.907
PDB ID: 6WBS      Human CFTR first nucleotide binding domain with dF508/V510D
Method X-ray diffraction Resolution 1.86 Å Mutation Yes [13]
PDB Sequence
TTTEVVMENV
429
TAFWEEGGTP
439
VLKDINFKIE
449
RGQLLAVAGS
459
TGAGKTSLLM
469

VIMGELEPSE
479
GKIKHSGRIS
489
FCSQFSWIMP
499
GTIKENIIGD
510
SYDEYRYRSV
520

IKACQLEEDI
530
SKFAEKDNIV
540
LGEGGITLSG
550
GQRARISLAR
560
AVYKDADLYL
570

LDSPFGYLDV
580
LTEKEIFESC
590
VCKLMANKTR
600
ILVTSKMEHL
610
KKADKILILH
620

EGSSYFYGTF
630
SELQN
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ATP or .ATP2 or .ATP3 or :3ATP;style chemicals stick;color identity;select .A:433 or .A:434 or .A:440 or .A:458 or .A:459 or .A:460 or .A:461 or .A:462 or .A:463 or .A:464 or .A:465 or .A:466 or .A:467 or .A:469 or .A:493; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
TRP433
2.671
GLU434
4.002
VAL440
2.414
GLY458
4.977
SER459
3.894
THR460
2.138
GLY461
2.189
ALA462
2.797
Residue
Distance (Å)
GLY463
2.296
LYS464
2.007
THR465
2.094
SER466
2.000
LEU467
4.701
MET469
4.554
GLN493
2.804
References  Top
REF 1 Mechanism of CFTR correction by type I folding correctors. Cell. 2022 Jan 6;185(1):158-168.e11.
REF 2 Molecular structures reveal synergistic rescue of Delta508 CFTR by Trikafta modulators. Science. 2022 Oct 21;378(6617):284-290.
REF 3 Molecular structure of the ATP-bound, phosphorylated human CFTR. Proc Natl Acad Sci U S A. 2018 Dec 11;115(50):12757-12762.
REF 4 Structural identification of a hotspot on CFTR for potentiation. Science. 2019 Jun 21;364(6446):1184-1188.
REF 5 Impact of the deltaF508 mutation in first nucleotide-binding domain of human cystic fibrosis transmembrane conductance regulator on domain folding and structure. J Biol Chem. 2005 Jan 14;280(2):1346-53.
REF 6 Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry. J Mol Biol. 2010 Feb 19;396(2):406-30.
REF 7 Binding screen for cystic fibrosis transmembrane conductance regulator correctors finds new chemical matter and yields insights into cystic fibrosis therapeutic strategy. Protein Sci. 2016 Feb;25(2):360-73.
REF 8 Domain-interface dynamics of CFTR revealed by stabilizing nanobodies. Nat Commun. 2019 Jun 14;10(1):2636.
REF 9 A topological switch in CFTR modulates channel activity and sensitivity to unfolding. Nat Chem Biol. 2021 Sep;17(9):989-997.
REF 10 Structures of a minimal human CFTR first nucleotide-binding domain as a monomer, head-to-tail homodimer, and pathogenic mutant. Protein Eng Des Sel. 2010 May;23(5):375-84.
REF 11 Thermodynamic correction of F508del-CFTR by ligand binding to a remote site in the mutated domain
REF 12 A thermodynamically stabilized form of the second nucleotide binding domain from human CFTR shows a catalytically inactive conformation
REF 13 Determining the Molecular Mechanism of Suppressor Mutation V510D and the Contribution of Helical Unraveling to the dF508-CFTR Defect

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