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 T83875 Target Info
Target Name Monoamine oxidase type A (MAO-A)
Synonyms Monoamine oxidase A; Amine oxidase [flavin-containing] A
Target Type Successful Target
Gene Name MAOA
Biochemical Class CH-NH(2) donor oxidoreductase
UniProt ID
AOFA_HUMAN
Ligand General Information  Top
Ligand Name Flavin-Adenine Dinucleotide Ligand Info
Canonical SMILES CC1=CC2=C(C=C1C)N(C3=NC(=O)NC(=O)C3=N2)CC(C(C(COP(=O)(O)OP(=O)(O)OCC4C(C(C(O4)N5C=NC6=C(N=CN=C65)N)O)O)O)O)O
InChI 1S/C27H33N9O15P2/c1-10-3-12-13(4-11(10)2)35(24-18(32-12)25(42)34-27(43)33-24)5-14(37)19(39)15(38)6-48-52(44,45)51-53(46,47)49-7-16-20(40)21(41)26(50-16)36-9-31-17-22(28)29-8-30-23(17)36/h3-4,8-9,14-16,19-21,26,37-41H,5-7H2,1-2H3,(H,44,45)(H,46,47)(H2,28,29,30)(H,34,42,43)/t14-,15+,16+,19-,20+,21+,26+/m0/s1
InChIKey VWWQXMAJTJZDQX-UYBVJOGSSA-N
PubChem Compound ID 643975
Drug Binding Sites of Target  Top
PDB ID: 2BXR      Human Monoamine Oxidase A in complex with Clorgyline, Crystal Form A
Method X-ray diffraction Resolution 3.00 Å Mutation No [1]
PDB Sequence
HMFDVVVIGG
21
GISGLSAAKL
31
LTEYGVSVLV
41
LEARDRVGGR
51
TYTIRNEHVD
61

YVDVGGAYVG
71
PTQNRILRLS
81
KELGIETYKV
91
NVSERLVQYV
101
KGKTYPFRGW
116

NPIAYLDYNN
126
LWRTIDNMGK
136
EIPTDAPWEA
146
QHADKWDKMT
156
MKELIDKICW
166

TKTARRFAYL
176
FVNINVTSEP
186
HEVSALWFLW
196
YVKQCGGTTR
206
IFSVGQERKF
219

VGGSGQVSER
229
IMDLLGDQVK
239
LNHPVTHVDQ
249
SSDNIIIETL
259
NHEHYECKYV
269

INAIPPTLTA
279
KIHFRPELPA
289
ERNQLIQRLP
299
MGAVIKCMMY
309
YKEAFWKKKD
319

YCGCMIIEDE
329
DAPISITLDD
339
TKPDGSLPAI
349
MGFILARKAD
359
RLAKLHKEIR
369

KKKICELYAK
379
VLGSQEALHP
389
VHYEEKNWCE
399
EQYSGGCYTA
409
YFPPGIMTQY
419

GRVIRQPVGR
429
IFFAGTETAT
439
KWSGYMEGAV
449
EAGERAAREV
459
LNGLG
Residue
Distance (Å)
ILE19
3.631
GLY20
3.181
GLY21
3.779
GLY22
3.313
ILE23
3.546
SER24
3.070
GLY25
4.420
LEU42
3.187
GLU43
2.420
ALA44
2.938
ARG45
3.078
ARG47
4.655
VAL48
4.925
GLY49
3.641
GLY50
3.406
ARG51
2.786
THR52
3.642
VAL65
3.910
GLY66
3.519
GLY67
3.236
ALA68
3.260
TYR69
2.787
VAL70
4.963
HIS242
3.704
Residue
Distance (Å)
PRO243
3.464
VAL244
2.880
ALA272
3.626
ILE273
3.101
PRO274
4.446
LEU277
3.657
ILE281
4.079
VAL303
4.102
LYS305
3.925
PHE352
3.858
TRP397
3.012
TYR402
3.471
SER403
3.969
CYS406
1.746
TYR407
3.691
GLY434
3.445
THR435
2.906
GLU436
4.772
GLY443
2.132
TYR444
3.311
MET445
2.637
GLU446
4.329
ALA448
3.560
PDB ID: 2BXS      Human Monoamine Oxidase A in complex with Clorgyline, Crystal Form B
Method X-ray diffraction Resolution 3.15 Å Mutation No [1]
PDB Sequence
HMFDVVVIGG
21
GISGLSAAKL
31
LTEYGVSVLV
41
LEARDRVGGR
51
TYTIRNEHVD
61

YVDVGGAYVG
71
PTQNRILRLS
81
KELGIETYKV
91
NVSERLVQYV
101
KGKTYPFRGW
116

NPIAYLDYNN
126
LWRTIDNMGK
136
EIPTDAPWEA
146
QHADKWDKMT
156
MKELIDKICW
166

TKTARRFAYL
176
FVNINVTSEP
186
HEVSALWFLW
196
YVKQCGGTTR
206
IFSVTNGGQE
216

RKFVGGSGQV
226
SERIMDLLGD
236
QVKLNHPVTH
246
VDQSSDNIII
256
ETLNHEHYEC
266

KYVINAIPPT
276
LTAKIHFRPE
286
LPAERNQLIQ
296
RLPMGAVIKC
306
MMYYKEAFWK
316

KKDYCGCMII
326
EDEDAPISIT
336
LDDTKPDGSL
346
PAIMGFILAR
356
KADRLAKLHK
366

EIRKKKICEL
376
YAKVLGSQEA
386
LHPVHYEEKN
396
WCEEQYSGGC
406
YTAYFPPGIM
416

TQYGRVIRQP
426
VGRIFFAGTE
436
TATKWSGYME
446
GAVEAGERAA
456
REVLNGLGKV
466

TEKDIWVQEP
476
ESKDVPAVEI
486
THTFWERNLP
496
SVSGLLKIIG
506
Residue
Distance (Å)
ILE19
3.316
GLY20
3.440
GLY21
3.943
GLY22
3.215
ILE23
3.277
SER24
3.170
GLY25
4.604
LEU42
3.608
GLU43
2.521
ALA44
3.553
ARG45
3.629
GLY49
4.029
GLY50
3.392
ARG51
2.775
THR52
3.960
VAL65
4.261
GLY66
3.668
GLY67
3.670
ALA68
3.326
TYR69
2.811
HIS242
3.598
PRO243
3.535
Residue
Distance (Å)
VAL244
2.692
ALA272
4.151
ILE273
3.451
PRO274
4.181
LEU277
4.016
ILE281
4.745
VAL303
4.407
LYS305
3.760
PHE352
4.114
TRP397
3.514
TYR402
3.601
SER403
4.519
CYS406
1.622
TYR407
3.385
GLY434
3.624
THR435
3.029
GLY443
2.519
TYR444
3.132
MET445
2.754
GLU446
4.100
ALA448
3.890
PDB ID: 2Z5Y      Crystal Structure of Human Monoamine Oxidase A (G110A) with Harmine
Method X-ray diffraction Resolution 2.17 Å Mutation Yes [2]
PDB Sequence
HMFDVVVIGG
21
GISGLSAAKL
31
LTEYGVSVLV
41
LEARDRVGGR
51
TYTIRNEHVD
61

YVDVGGAYVG
71
PTQNRILRLS
81
KELGIETYKV
91
NVSERLVQYV
101
KGKTYPFRAA
111

FPPVWNPIAY
121
LDYNNLWRTI
131
DNMGKEIPTD
141
APWEAQHADK
151
WDKMTMKELI
161

DKICWTKTAR
171
RFAYLFVNIN
181
VTSEPHEVSA
191
LWFLWYVKQC
201
GGTTRIFSVT
211

NGGQERKFVG
221
GSGQVSERIM
231
DLLGDQVKLN
241
HPVTHVDQSS
251
DNIIIETLNH
261

EHYECKYVIN
271
AIPPTLTAKI
281
HFRPELPAER
291
NQLIQRLPMG
301
AVIKCMMYYK
311

EAFWKKKDYC
321
GCMIIEDEDA
331
PISITLDDTK
341
PDGSLPAIMG
351
FILARKADRL
361

AKLHKEIRKK
371
KICELYAKVL
381
GSQEALHPVH
391
YEEKNWCEEQ
401
YSGGCYTAYF
411

PPGIMTQYGR
421
VIRQPVGRIF
431
FAGTETATKW
441
SGYMEGAVEA
451
GERAAREVLN
461

GLGKVTEKDI
471
WVQEPESKDV
481
PAVEITHTFW
491
ERNLPSVSGL
501
LKIIGFSTSV
511

TALGFVLYKY
521
KLL
Residue
Distance (Å)
ILE19
3.571
GLY20
3.372
GLY21
3.594
GLY22
3.323
ILE23
3.144
SER24
2.655
GLY25
4.173
LEU42
3.235
GLU43
2.596
ALA44
3.096
ARG45
2.965
ARG47
4.860
VAL48
4.938
GLY49
3.632
GLY50
3.014
ARG51
2.792
THR52
3.770
VAL65
3.633
GLY66
3.639
GLY67
3.322
ALA68
3.297
TYR69
2.961
GLN74
4.892
HIS242
3.835
Residue
Distance (Å)
PRO243
3.638
VAL244
2.932
ALA272
3.572
ILE273
3.222
PRO274
3.830
LEU277
3.651
ILE281
4.475
VAL303
3.832
LYS305
3.913
PHE352
4.234
TRP397
3.203
TYR402
3.390
SER403
4.729
CYS406
1.812
TYR407
3.365
GLY434
3.346
THR435
2.711
GLU436
4.522
GLY443
2.689
TYR444
3.325
MET445
2.711
GLU446
4.337
ALA448
3.457
PDB ID: 2Z5X      Crystal Structure of Human Monoamine Oxidase A with Harmine
Method X-ray diffraction Resolution 2.20 Å Mutation No [2]
PDB Sequence
HMFDVVVIGG
21
GISGLSAAKL
31
LTEYGVSVLV
41
LEARDRVGGR
51
TYTIRNEHVD
61

YVDVGGAYVG
71
PTQNRILRLS
81
KELGIETYKV
91
NVSERLVQYV
101
KGKTYPFRGA
111

FPPVWNPIAY
121
LDYNNLWRTI
131
DNMGKEIPTD
141
APWEAQHADK
151
WDKMTMKELI
161

DKICWTKTAR
171
RFAYLFVNIN
181
VTSEPHEVSA
191
LWFLWYVKQC
201
GGTTRIFSVT
211

NGGQERKFVG
221
GSGQVSERIM
231
DLLGDQVKLN
241
HPVTHVDQSS
251
DNIIIETLNH
261

EHYECKYVIN
271
AIPPTLTAKI
281
HFRPELPAER
291
NQLIQRLPMG
301
AVIKCMMYYK
311

EAFWKKKDYC
321
GCMIIEDEDA
331
PISITLDDTK
341
PDGSLPAIMG
351
FILARKADRL
361

AKLHKEIRKK
371
KICELYAKVL
381
GSQEALHPVH
391
YEEKNWCEEQ
401
YSGGCYTAYF
411

PPGIMTQYGR
421
VIRQPVGRIF
431
FAGTETATKW
441
SGYMEGAVEA
451
GERAAREVLN
461

GLGKVTEKDI
471
WVQEPESKDV
481
PAVEITHTFW
491
ERNLPSVSGL
501
LKIIGFSTSV
511

TALGFVLYKY
521
KLL
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .FAD or .FAD2 or .FAD3 or :3FAD;style chemicals stick;color identity;select .A:19 or .A:20 or .A:21 or .A:22 or .A:23 or .A:24 or .A:25 or .A:42 or .A:43 or .A:44 or .A:45 or .A:47 or .A:48 or .A:49 or .A:50 or .A:51 or .A:52 or .A:65 or .A:66 or .A:67 or .A:68 or .A:69 or .A:74 or .A:242 or .A:243 or .A:244 or .A:272 or .A:273 or .A:274 or .A:277 or .A:281 or .A:303 or .A:305 or .A:352 or .A:397 or .A:402 or .A:403 or .A:406 or .A:407 or .A:434 or .A:435 or .A:436 or .A:443 or .A:444 or .A:445 or .A:446 or .A:448; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
Residue
Distance (Å)
ILE19
3.480
GLY20
3.310
GLY21
3.820
GLY22
3.211
ILE23
3.198
SER24
2.645
GLY25
4.295
LEU42
3.050
GLU43
2.616
ALA44
3.019
ARG45
2.790
ARG47
4.739
VAL48
4.977
GLY49
3.626
GLY50
3.150
ARG51
2.782
THR52
3.528
VAL65
3.782
GLY66
3.649
GLY67
3.246
ALA68
3.221
TYR69
3.002
GLN74
4.875
HIS242
3.747
Residue
Distance (Å)
PRO243
3.577
VAL244
2.921
ALA272
3.567
ILE273
3.395
PRO274
4.044
LEU277
3.407
ILE281
4.372
VAL303
3.646
LYS305
4.142
PHE352
4.414
TRP397
3.407
TYR402
3.374
SER403
4.598
CYS406
1.653
TYR407
3.262
GLY434
3.158
THR435
2.682
GLU436
4.583
GLY443
3.054
TYR444
3.275
MET445
2.603
GLU446
4.308
ALA448
3.500
References  Top
REF 1 Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B. Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12684-9.
REF 2 Structure of human monoamine oxidase A at 2.2-A resolution: the control of opening the entry for substrates/inhibitors. Proc Natl Acad Sci U S A. 2008 Apr 15;105(15):5739-44.

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