Target Binding Site Detail
| 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 | |||||
| Ligand General Information | Top | ||||
|---|---|---|---|---|---|
| Ligand Name | Glutathione | Ligand Info | |||
| Canonical SMILES | C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N | ||||
| InChI | 1S/C10H17N3O6S/c11-5(10(18)19)1-2-7(14)13-6(4-20)9(17)12-3-8(15)16/h5-6,20H,1-4,11H2,(H,12,17)(H,13,14)(H,15,16)(H,18,19)/t5-,6-/m0/s1 | ||||
| InChIKey | RWSXRVCMGQZWBV-WDSKDSINSA-N | ||||
| PubChem Compound ID | 124886 | ||||
| Drug Binding Sites of Target | Top | |||||
|---|---|---|---|---|---|---|
| PDB ID: 3DK8 Catalytic cycle of human glutathione reductase near 1 A resolution | ||||||
| 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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| PDB ID: 3DK4 Catalytic cycle of human glutathione reductase near 1 A resolution | ||||||
| Method | X-ray diffraction | Resolution | 1.20 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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| PDB ID: 1DNC HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DIGLUTATHIONE-DINITROSO-IRON | ||||||
| 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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| PDB ID: 1GSN HUMAN GLUTATHIONE REDUCTASE MODIFIED BY DINITROSOGLUTATHIONE | ||||||
| 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 .GSH or .GSH2 or .GSH3 or :3GSH;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: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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| PDB ID: 1GRA SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION | ||||||
| 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 .GSH or .GSH2 or .GSH3 or :3GSH;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 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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| PDB ID: 1GRE SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION | ||||||
| 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 .GSH or .GSH2 or .GSH3 or :3GSH;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 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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| 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. | ||||
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