Binding Site Information of Target
| Target General Information | Top | ||||
|---|---|---|---|---|---|
| Target ID | T30803 | Target Info | |||
| Target Name | Glutathione reductase (GR) | ||||
| Synonyms | Glutathione reductase, mitochondrial; GRase; GRD1; GLUR | ||||
| Target Type | Patented-recorded Target | ||||
| Gene Name | GSR | ||||
| Biochemical Class | Sulfur donor oxidoreductase | ||||
| UniProt ID | |||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| Ligand Name: Glutathione | Ligand Info | |||||
| Structure Description | Catalytic cycle of human glutathione reductase near 1 A resolution | PDB:3DK8 | ||||
| Method | X-ray diffraction | Resolution | 1.10 Å | Mutation | No | [1] |
| PDB Sequence |
AVASYDYLVI
26 GGGSGGLASA36 RRAAELGARA46 AVVESHKLGG56 TCVNVGCVPK66 KVMWNTAVHS 76 EFMHDHADYG86 FPSCEGKFNW96 RVIKEKRDAY106 VSRLNAIYQN116 NLTKSHIEII 126 RGHAAFTSDP136 KPTIEVSGKK146 YTAPHILIAT156 GGMPSTPHES166 QIPGASLGIT 176 SDGFFQLEEL186 PGRSVIVGAG196 YIAVEMAGIL206 SALGSKTSLM216 IRHDKVLRSF 226 DSMISTNCTE236 ELENAGVEVL246 KFSQVKEVKK256 TLSGLEVSMV266 TAVPGRLPVM 276 TMIPDVDCLL286 WAIGRVPNTK296 DLSLNKLGIQ306 TDDKGHIIVD316 EFQNTNVKGI 326 YAVGDVCGKA336 LLTPVAIAAG346 RKLAHRLFEY356 KEDSKLDYNN366 IPTVVFSHPP 376 IGTVGLTEDE386 AIHKYGIENV396 KTYSTSFTPM406 YHAVTKRKTK416 CVMKMVCANK 426 EEKVVGIHMQ436 GLGCDEMLQG446 FAVAVKMGAT456 KADFDNTVAI466 HPTSSEELVT 476 LR
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: Flavin-Adenine Dinucleotide | Ligand Info | |||||
| Structure Description | Catalytic cycle of human glutathione reductase near 1 A resolution | PDB:3DK9 | ||||
| Method | X-ray diffraction | Resolution | 0.95 Å | Mutation | No | [1] |
| PDB Sequence |
AVASYDYLVI
26 GGGSGGLASA36 RRAAELGARA46 AVVESHKLGG56 TCVNVGCVPK66 KVMWNTAVHS 76 EFMHDHADYG86 FPSCEGKFNW96 RVIKEKRDAY106 VSRLNAIYQN116 NLTKSHIEII 126 RGHAAFTSDP136 KPTIEVSGKK146 YTAPHILIAT156 GGMPSTPHES166 QIPGASLGIT 176 SDGFFQLEEL186 PGRSVIVGAG196 YIAVEMAGIL206 SALGSKTSLM216 IRHDKVLRSF 226 DSMISTNCTE236 ELENAGVEVL246 KFSQVKEVKK256 TLSGLEVSMV266 TAVPGRLPVM 276 TMIPDVDCLL286 WAIGRVPNTK296 DLSLNKLGIQ306 TDDKGHIIVD316 EFQNTNVKGI 326 YAVGDVCGKA336 LLTPVAIAAG346 RKLAHRLFEY356 KEDSKLDYNN366 IPTVVFSHPP 376 IGTVGLTEDE386 AIHKYGIENV396 KTYSTSFTPM406 YHAVTKRKTK416 CVMKMVCANK 426 EEKVVGIHMQ436 GLGCDEMLQG446 FAVAVKMGAT456 KADFDNTVAI466 HPTSSEELVT 476 LR
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ILE26
3.753
GLY27
3.254
GLY28
4.052
GLY29
3.315
SER30
3.250
GLY31
2.836
GLY32
4.159
VAL49
3.708
GLU50
2.658
SER51
3.174
HIS52
3.794
LYS53
3.666
GLY55
4.134
GLY56
3.214
THR57
2.789
CYS58
3.362
VAL61
3.733
GLY62
3.635
CYS63
3.261
LYS66
2.736
GLY128
3.361
HIS129
3.261
ALA130
3.010
ALA155
3.315
THR156
3.401
GLY157
3.364
GLY158
4.391
SER177
3.808
PHE181
4.248
TYR197
3.109
ILE198
3.981
GLU201
4.621
MET202
3.939
ARG291
3.385
ASN294
3.534
LEU298
3.616
VAL329
4.270
GLY330
3.385
ASP331
2.801
VAL332
4.507
LEU337
3.290
LEU338
3.144
THR339
2.943
PRO340
3.097
ALA342
3.955
PHE372
4.291
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: NADPH | Ligand Info | |||||
| Structure Description | Catalytic cycle of human glutathione reductase near 1 A resolution | PDB:3DJJ | ||||
| Method | X-ray diffraction | Resolution | 1.10 Å | Mutation | No | [1] |
| PDB Sequence |
AVASYDYLVI
26 GGGSGGLASA36 RRAAELGARA46 AVVESHKLGG56 TCVNVGCVPK66 KVMWNTAVHS 76 EFMHDHADYG86 FPSCEGKFNW96 RVIKEKRDAY106 VSRLNAIYQN116 NLTKSHIEII 126 RGHAAFTSDP136 KPTIEVSGKK146 YTAPHILIAT156 GGMPSTPHES166 QIPGASLGIT 176 SDGFFQLEEL186 PGRSVIVGAG196 YIAVEMAGIL206 SALGSKTSLM216 IRHDKVLRSF 226 DSMISTNCTE236 ELENAGVEVL246 KFSQVKEVKK256 TLSGLEVSMV266 TAVPGRLPVM 276 TMIPDVDCLL286 WAIGRVPNTK296 DLSLNKLGIQ306 TDDKGHIIVD316 EFQNTNVKGI 326 YAVGDVCGKA336 LLTPVAIAAG346 RKLAHRLFEY356 KEDSKLDYNN366 IPTVVFSHPP 376 IGTVGLTEDE386 AIHKYGIENV396 KTYSTSFTPM406 YHAVTKRKTK416 CVMKMVCANK 426 EEKVVGIHMQ436 GLGCDEMLQG446 FAVAVKMGAT456 KADFDNTVAI466 HPTSSEELVT 476 LR
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NDP or .NDP2 or .NDP3 or :3NDP;style chemicals stick;color identity;select .A:66 or .A:193 or .A:194 or .A:195 or .A:196 or .A:197 or .A:198 or .A:199 or .A:201 or .A:218 or .A:219 or .A:221 or .A:224 or .A:250 or .A:288 or .A:289 or .A:290 or .A:291 or .A:337 or .A:338 or .A:369 or .A:370 or .A:371 or .A:372; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
LYS66
3.770
VAL193
4.101
GLY194
3.805
ALA195
3.221
GLY196
3.228
TYR197
3.327
ILE198
2.874
ALA199
4.261
GLU201
2.942
ARG218
2.813
HIS219
3.767
LYS221
4.510
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| Click to View More Binding Site Information of This Target and Ligand Pair | ||||||
| Ligand Name: 3-Sulfinoalanine | Ligand Info | |||||
| Structure Description | HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DIGLUTATHIONE-DINITROSO-IRON | PDB:1DNC | ||||
| Method | X-ray diffraction | Resolution | 1.70 Å | Mutation | No | [2] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGVPKKV68 MWNTAVHSEF 78 MHDHADYGFP88 SCEGKFNWRV98 IKEKRDAYVS108 RLNAIYQNNL118 TKSHIEIIRG 128 HAAFTSDPKP138 TIEVSGKKYT148 APHILIATGG158 MPSTPHESQI168 PGASLGITSD 178 GFFQLEELPG188 RSVIVGAGYI198 AVEMAGILSA208 LGSKTSLMIR218 HDKVLRSFDS 228 MISTNCTEEL238 ENAGVEVLKF248 SQVKEVKKTL258 SGLEVSMVTA268 VPGRLPVMTM 278 IPDVDCLLWA288 IGRVPNTKDL298 SLNKLGIQTD308 DKGHIIVDEF318 QNTNVKGIYA 328 VGDVCGKALL338 TPVAIAAGRK348 LAHRLFEYKE358 DSKLDYNNIP368 TVVFSHPPIG 378 TVGLTEDEAI388 HKYGIENVKT398 YSTSFTPMYH408 AVTKRKTKCV418 MKMVCANKEE 428 KVVGIHMQGL438 GCDEMLQGFA448 VAVKMGATKA458 DFDNTVAIHP468 TSSEELVTLR 478
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CSD or .CSD2 or .CSD3 or :3CSD;style chemicals stick;color identity;select .A:57 or .A:58 or .A:61 or .A:62 or .A:64 or .A:65 or .A:66 or .A:67 or .A:339 or .A:340; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: Cysteine Sulfenic Acid | Ligand Info | |||||
| Structure Description | HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DINITROSOGLUTATHIONE | PDB:1GSN | ||||
| Method | X-ray diffraction | Resolution | 1.70 Å | Mutation | No | [2] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGVPKKV68 MWNTAVHSEF 78 MHDHADYGFP88 SCEGKFNWRV98 IKEKRDAYVS108 RLNAIYQNNL118 TKSHIEIIRG 128 HAAFTSDPKP138 TIEVSGKKYT148 APHILIATGG158 MPSTPHESQI168 PGASLGITSD 178 GFFQLEELPG188 RSVIVGAGYI198 AVEMAGILSA208 LGSKTSLMIR218 HDKVLRSFDS 228 MISTNTEELE239 NAGVEVLKFS249 QVKEVKKTLS259 GLEVSMVTAV269 PGRLPVMTMI 279 PDVDLLWAIG290 RVPNTKDLSL300 NKLGIQTDDK310 GHIIVDEFQN320 TNVKGIYAVG 330 DVCGKALLTP340 VAIAAGRKLA350 HRLFEYKEDS360 KLDYNNIPTV370 VFSHPPIGTV 380 GLTEDEAIHK390 YGIENVKTYS400 TSFTPMYHAV410 TKRKTKCVMK420 MVANKEEKVV 431 GIHMQGLGCD441 EMLQGFAVAV451 KMGATKADFD461 NTVAIHPTSS471 EELVTLR |
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .CSO or .CSO2 or .CSO3 or :3CSO;style chemicals stick;color identity;select .A:57 or .A:58 or .A:61 or .A:62 or .A:64 or .A:65 or .A:66 or .A:67 or .A:175 or .A:183 or .A:187 or .A:189 or .A:190 or .A:191 or .A:200 or .A:206 or .A:222 or .A:223 or .A:229 or .A:230 or .A:231 or .A:232 or .A:233 or .A:235 or .A:236 or .A:237 or .A:238 or .A:282 or .A:283 or .A:285 or .A:286 or .A:339 or .A:373 or .A:377 or .A:395 or .A:396 or .A:397 or .A:398 or .A:399 or .A:421 or .A:422 or .A:424 or .A:425 or .A:428 or .A:429 or .A:430 or .A:431 or .A:436 or .A:457; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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THR57
4.190
CYS58
3.057
VAL61
4.659
GLY62
1.327
VAL64
1.333
PRO65
3.790
LYS66
3.582
LYS67
2.946
ILE175
2.824
LEU183
4.506
PRO187
3.538
ARG189
3.080
SER190
3.223
VAL191
2.888
VAL200
3.267
LEU206
4.844
VAL222
3.229
LEU223
3.169
MET229
4.888
ILE230
2.810
SER231
3.685
THR232
3.261
ASN233
1.324
THR235
1.333
GLU236
3.279
GLU237
3.461
LEU238
3.080
VAL282
3.404
ASP283
1.327
LEU285
1.333
LEU286
3.962
THR339
3.228
SER373
4.512
ILE377
3.884
ASN395
3.832
VAL396
3.514
LYS397
2.777
THR398
4.805
TYR399
2.773
MET421
3.682
VAL422
1.334
ALA424
1.329
ASN425
4.469
GLU428
3.761
LYS429
3.117
VAL430
4.370
VAL431
4.483
GLN436
3.453
LYS457
4.067
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| Ligand Name: Nicotinamide-Adenine-Dinucleotide | Ligand Info | |||||
| Structure Description | SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION | PDB:1GRB | ||||
| Method | X-ray diffraction | Resolution | 1.85 Å | Mutation | No | [3] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NAD or .NAD2 or .NAD3 or :3NAD;style chemicals stick;color identity;select .A:66 or .A:193 or .A:194 or .A:195 or .A:196 or .A:197 or .A:198 or .A:199 or .A:201 or .A:218 or .A:288 or .A:289 or .A:290 or .A:291 or .A:337 or .A:338 or .A:369 or .A:370 or .A:371 or .A:372; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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LYS66
3.578
VAL193
3.897
GLY194
3.704
ALA195
3.498
GLY196
3.277
TYR197
3.301
ILE198
2.960
ALA199
4.303
GLU201
2.628
ARG218
3.234
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| Ligand Name: Acetamide | Ligand Info | |||||
| Structure Description | SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION | PDB:1GRF | ||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [3] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ACM or .ACM2 or .ACM3 or :3ACM;style chemicals stick;color identity;select .A:30 or .A:55 or .A:58 or .A:59 or .A:63 or .A:64 or .A:114; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: 3-(Prop-2-Ene-1-Sulfinyl)-Propene-1-Thiol | Ligand Info | |||||
| Structure Description | STRUCTURE OF HUMAN GLUTATHIONE REDUCTASE COMPLEXED with AJOENE INHIBITOR AND SUBVERSIVE SUBSTRATE | PDB:1BWC | ||||
| Method | X-ray diffraction | Resolution | 2.10 Å | Mutation | No | [4] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .AJ3 or .AJ32 or .AJ33 or :3AJ3;style chemicals stick;color identity;select .A:29 or .A:30 or .A:31 or .A:33 or .A:34 or .A:37 or .A:55 or .A:58 or .A:59 or .A:114 or .A:339 or .A:343 or .A:347; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: Meta-Nitro-Tyrosine | Ligand Info | |||||
| Structure Description | Human Glutathione Reductase Inactivated by Peroxynitrite | PDB:1K4Q | ||||
| Method | X-ray diffraction | Resolution | 1.90 Å | Mutation | Yes | [5] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .NIY or .NIY2 or .NIY3 or :3NIY;style chemicals stick;color identity;select .A:28 or .A:29 or .A:30 or .A:33 or .A:54 or .A:55 or .A:56 or .A:59 or .A:64 or .A:68 or .A:102 or .A:103 or .A:104 or .A:105 or .A:106 or .A:107 or .A:108 or .A:109 or .A:110 or .A:111 or .A:112 or .A:113 or .A:114 or .A:115 or .A:116 or .A:117 or .A:118; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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GLY28
4.518
GLY29
3.983
SER30
4.193
LEU33
3.044
LEU54
4.564
GLY55
3.118
GLY56
4.805
VAL59
4.092
VAL64
3.678
VAL68
4.028
LYS102
3.078
ARG103
3.079
ASP104
3.267
ALA105
1.339
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| Ligand Name: 3,6-Dihydroxy-Xanthene-9-Propionic Acid | Ligand Info | |||||
| Structure Description | HUMAN GLUTATHIONE REDUCTASE IN COMPLEX WITH A XANTHENE INHIBITOR | PDB:1XAN | ||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [6] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .HXP or .HXP2 or .HXP3 or :3HXP;style chemicals stick;color identity;select .A:70 or .A:71 or .A:74 or .A:75 or .A:78 or .A:79 or .A:82 or .A:407; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: Glutathionylspermidine Disulfide | Ligand Info | |||||
| Structure Description | HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, GLUTATHIONYLSPERMIDINE COMPLEX | PDB:5GRT | ||||
| Method | X-ray diffraction | Resolution | 2.40 Å | Mutation | Yes | [7] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLESAW37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .TS4 or .TS42 or .TS43 or :3TS4;style chemicals stick;color identity;select .A:29 or .A:30 or .A:33 or .A:34 or .A:37 or .A:55 or .A:58 or .A:59 or .A:63 or .A:64 or .A:106 or .A:110 or .A:113 or .A:114 or .A:117 or .A:339 or .A:343; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: Trypanothione | Ligand Info | |||||
| Structure Description | HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, OXIDIZED TRYPANOTHIONE COMPLEX | PDB:3GRT | ||||
| Method | X-ray diffraction | Resolution | 2.50 Å | Mutation | Yes | [7] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLESAW37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .TS2 or .TS22 or .TS23 or :3TS2;style chemicals stick;color identity;select .A:29 or .A:30 or .A:33 or .A:34 or .A:37 or .A:55 or .A:58 or .A:59 or .A:64 or .A:106 or .A:110 or .A:113 or .A:114 or .A:117 or .A:339 or .A:343; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: 2-(2-Phenyl-3-pyridin-2-YL-4,5,6,7-tetrahydro-2H-isophosphindol-1-YL)pyridine | Ligand Info | |||||
| Structure Description | Crystal Structure Analysis of the human Glutahione Reductase, complexed with GoPI | PDB:2AAQ | ||||
| Method | X-ray diffraction | Resolution | 2.60 Å | Mutation | No | [8] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .AUP or .AUP2 or .AUP3 or :3AUP;style chemicals stick;color identity;select .A:172 or .A:173 or .A:174 or .A:175 or .A:179 or .A:180 or .A:182 or .A:183 or .A:260 or .A:261 or .A:282 or .A:283 or .A:284; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: 6-(3-Methyl-1,4-Dioxo-1,4-Dihydronaphthalen-2-Yl)hexanoic Acid | Ligand Info | |||||
| Structure Description | Crystal Structure of human Glutathione Reductase complexed with a Fluoro-Analogue of the Menadione Derivative M5 | PDB:2GH5 | ||||
| Method | X-ray diffraction | Resolution | 1.70 Å | Mutation | No | [9] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .ELI or .ELI2 or .ELI3 or :3ELI;style chemicals stick;color identity;select .A:29 or .A:30 or .A:33 or .A:34 or .A:37 or .A:55 or .A:58 or .A:59 or .A:64 or .A:110 or .A:113 or .A:114 or .A:339 or .A:343 or .A:347; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: S-[(2-Chloroethyl)carbamoyl]-L-cysteine | Ligand Info | |||||
| Structure Description | SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION | PDB:1GRG | ||||
| Method | X-ray diffraction | Resolution | 2.00 Å | Mutation | No | [3] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 VNVGCVPKKV68 MWNTAVHSEF 78 MHDHADYGFP88 SCEGKFNWRV98 IKEKRDAYVS108 RLNAIYQNNL118 TKSHIEIIRG 128 HAAFTSDPKP138 TIEVSGKKYT148 APHILIATGG158 MPSTPHESQI168 PGASLGITSD 178 GFFQLEELPG188 RSVIVGAGYI198 AVEMAGILSA208 LGSKTSLMIR218 HDKVLRSFDS 228 MISTNCTEEL238 ENAGVEVLKF248 SQVKEVKKTL258 SGLEVSMVTA268 VPGRLPVMTM 278 IPDVDCLLWA288 IGRVPNTKDL298 SLNKLGIQTD308 DKGHIIVDEF318 QNTNVKGIYA 328 VGDVCGKALL338 TPVAIAAGRK348 LAHRLFEYKE358 DSKLDYNNIP368 TVVFSHPPIG 378 TVGLTEDEAI388 HKYGIENVKT398 YSTSFTPMYH408 AVTKRKTKCV418 MKMVCANKEE 428 KVVGIHMQGL438 GCDEMLQGFA448 VAVKMGATKA458 DFDNTVAIHP468 TSSEELVTLR 478
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .0A8 or .0A82 or .0A83 or :30A8;style chemicals stick;color identity;select .A:30 or .A:55 or .A:56 or .A:57 or .A:59 or .A:60 or .A:61 or .A:62 or .A:63 or .A:64 or .A:65 or .A:110 or .A:114 or .A:339; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: Pyocyanine | Ligand Info | |||||
| Structure Description | Structure of human glutathione reductase complexed with pyocyanin, an agent with antimalarial activity | PDB:3SQP | ||||
| Method | X-ray diffraction | Resolution | 2.21 Å | Mutation | No | [10] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .3J8 or .3J82 or .3J83 or :33J8;style chemicals stick;color identity;select .A:71 or .A:74 or .A:75 or .A:78 or .A:407; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: 4n-Malonyl-Cysteinyl-2,4-Diaminobutyrate Disulfide | Ligand Info | |||||
| Structure Description | THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASE | PDB:4GR1 | ||||
| Method | X-ray diffraction | Resolution | 2.40 Å | Mutation | No | [11] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLASAR37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .RGS or .RGS2 or .RGS3 or :3RGS;style chemicals stick;color identity;select .A:58 or .A:59 or .A:64 or .A:106 or .A:110 or .A:113 or .A:114 or .A:339 or .A:343 or .A:347; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| Ligand Name: (2S)-2-azaniumyl-5-[[(2R)-3-[[(2R)-2-[[(4S)-4-azaniumyl-4-carboxylatobutanoyl]amino]-3-(carboxymethylamino)-3-oxopropyl]disulfanyl]-1-(carboxymethylamino)-1-oxopropan-2-yl]amino]-5-oxopentanoate | Ligand Info | |||||
| Structure Description | HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, OXIDIZED GLUTATHIONE COMPLEX | PDB:2GRT | ||||
| Method | X-ray diffraction | Resolution | 2.70 Å | Mutation | Yes | [7] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLESAW37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
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|
Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GDS or .GDS2 or .GDS3 or :3GDS;style chemicals stick;color identity;select .A:29 or .A:30 or .A:33 or .A:34 or .A:37 or .A:55 or .A:58 or .A:59 or .A:64 or .A:106 or .A:110 or .A:113 or .A:114 or .A:117 or .A:339 or .A:340 or .A:343 or .A:347; color #f3c393; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
|
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| Ligand Name: Bis(gamma-glutamyl-cysteinyl-glycinyl)spermidine | Ligand Info | |||||
| Structure Description | HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, MIXED DISULFIDE BETWEEN TRYPANOTHIONE AND THE ENZYME | PDB:4GRT | ||||
| Method | X-ray diffraction | Resolution | 2.80 Å | Mutation | Yes | [7] |
| PDB Sequence |
VASYDYLVIG
27 GGSGGLESAW37 RAAELGARAA47 VVESHKLGGT57 CVNVGCVPKK67 VMWNTAVHSE 77 FMHDHADYGF87 PSCEGKFNWR97 VIKEKRDAYV107 SRLNAIYQNN117 LTKSHIEIIR 127 GHAAFTSDPK137 PTIEVSGKKY147 TAPHILIATG157 GMPSTPHESQ167 IPGASLGITS 177 DGFFQLEELP187 GRSVIVGAGY197 IAVEMAGILS207 ALGSKTSLMI217 RHDKVLRSFD 227 SMISTNCTEE237 LENAGVEVLK247 FSQVKEVKKT257 LSGLEVSMVT267 AVPGRLPVMT 277 MIPDVDCLLW287 AIGRVPNTKD297 LSLNKLGIQT307 DDKGHIIVDE317 FQNTNVKGIY 327 AVGDVCGKAL337 LTPVAIAAGR347 KLAHRLFEYK357 EDSKLDYNNI367 PTVVFSHPPI 377 GTVGLTEDEA387 IHKYGIENVK397 TYSTSFTPMY407 HAVTKRKTKC417 VMKMVCANKE 427 EKVVGIHMQG437 LGCDEMLQGF447 AVAVKMGATK457 ADFDNTVAIH467 PTSSEELVTL 477 R
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Click to Show 3D Structure of This Binding Site
set background white;style ions nothing; color 8e8e8e;style chemicals nothing; select .GCG or .GCG2 or .GCG3 or :3GCG;style chemicals stick;color identity;select .A:29 or .A:30 or .A:33 or .A:34 or .A:37 or .A:55 or .A:58 or .A:59 or .A:64 or .A:106 or .A:110 or .A:113 or .A:114 or .A:117 or .A:339 or .A:343; color #00ffc7; zoom selection;set surface opacity 0.5;set surface Van der Waals surface;set mode all
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| References | Top | ||||
|---|---|---|---|---|---|
| REF 1 | Catalytic cycle of human glutathione reductase near 1 A resolution. J Mol Biol. 2008 Oct 3;382(2):371-84. | ||||
| REF 2 | Enzyme inactivation through sulfhydryl oxidation by physiologic NO-carriers. Nat Struct Biol. 1998 Apr;5(4):267-71. | ||||
| REF 3 | Substrate binding and catalysis by glutathione reductase as derived from refined enzyme: substrate crystal structures at 2 A resolution. J Mol Biol. 1989 Nov 5;210(1):163-80. | ||||
| REF 4 | Ajoene is an inhibitor and subversive substrate of human glutathione reductase and Trypanosoma cruzi trypanothione reductase: crystallographic, kinetic, and spectroscopic studies. J Med Chem. 1999 Feb 11;42(3):364-72. | ||||
| REF 5 | Crystal structure of the antioxidant enzyme glutathione reductase inactivated by peroxynitrite. J Biol Chem. 2002 Jan 25;277(4):2779-84. | ||||
| REF 6 | Kinetics and crystallographic analysis of human glutathione reductase in complex with a xanthene inhibitor. J Biol Chem. 1996 Apr 5;271(14):8101-7. | ||||
| REF 7 | Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity. Biochemistry. 1997 May 27;36(21):6437-47. | ||||
| REF 8 | Undressing of phosphine gold(I) complexes as irreversible inhibitors of human disulfide reductases. Angew Chem Int Ed Engl. 2006 Mar 13;45(12):1881-6. | ||||
| REF 9 | A fluoro analogue of the menadione derivative 6-[2'-(3'-methyl)-1',4'-naphthoquinolyl]hexanoic acid is a suicide substrate of glutathione reductase. Crystal structure of the alkylated human enzyme. J Am Chem Soc. 2006 Aug 23;128(33):10784-94. | ||||
| REF 10 | The bacterial redox signaller pyocyanin as an antiplasmodial agent: comparisons with its thioanalog methylene blue. Redox Rep. 2011;16(4):154-65. | ||||
| REF 11 | The binding of the retro-analogue of glutathione disulfide to glutathione reductase. J Biol Chem. 1990 Jun 25;265(18):10443-5. | ||||
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