Structure of PDB 4grt Chain A Binding Site BS02

Receptor Information
>4grt Chain A (length=461) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VASYDYLVIGGGSGGLESAWRAAELGARAAVVESHKLGGTCVNVGCVPKK
VMWNTAVHSEFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNN
LTKSHIEIIRGHAAFTSDPKPTIEVSGKKYTAPHILIATGGMPSTPHESQ
IPGASLGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMI
RHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTLSGLEVSMVT
AVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDE
FQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNI
PTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKC
VMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIH
PTSSEELVTLR
Ligand information
Ligand IDGCG
InChIInChI=1S/C27H49N9O10S2/c28-16(26(43)44)4-6-20(37)35-18(14-47)24(41)33-12-22(39)31-10-2-1-8-30-9-3-11-32-23(40)13-34-25(42)19(15-48)36-21(38)7-5-17(29)27(45)46/h16-19,30,47-48H,1-15,28-29H2,(H,31,39)(H,32,40)(H,33,41)(H,34,42)(H,35,37)(H,36,38)(H,43,44)(H,45,46)/t16-,17-,18-,19-/m0/s1
InChIKeyPHDOXVGRXXAYEB-VJANTYMQSA-N
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.5.0C(CCNC(=O)CNC(=O)C(CS)NC(=O)CCC(C(=O)O)N)CNCCCNC(=O)CNC(=O)C(CS)NC(=O)CCC(C(=O)O)N
OpenEye OEToolkits 1.5.0C(CCNC(=O)CNC(=O)[C@H](CS)NC(=O)CC[C@@H](C(=O)O)N)CNCCCNC(=O)CNC(=O)[C@H](CS)NC(=O)CC[C@@H](C(=O)O)N
CACTVS 3.341N[CH](CCC(=O)N[CH](CS)C(=O)NCC(=O)NCCCCNCCCNC(=O)CNC(=O)[CH](CS)NC(=O)CC[CH](N)C(O)=O)C(O)=O
ACDLabs 10.04O=C(NCC(=O)NCCCNCCCCNC(=O)CNC(=O)C(NC(=O)CCC(C(=O)O)N)CS)C(NC(=O)CCC(C(=O)O)N)CS
CACTVS 3.341N[C@@H](CCC(=O)N[C@@H](CS)C(=O)NCC(=O)NCCCCNCCCNC(=O)CNC(=O)[C@H](CS)NC(=O)CC[C@H](N)C(O)=O)C(O)=O
FormulaC27 H49 N9 O10 S2
NameBIS(GAMMA-GLUTAMYL-CYSTEINYL-GLYCINYL)SPERMIDINE;
TRYPANOTHIONE
ChEMBL
DrugBankDB03470
ZINCZINC000008217540
PDB chain4grt Chain A Residue 17 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB4grt Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity.
Resolution2.8 Å
Binding residue
(original residue number in PDB)		S30 L33 E34 C58 V59 V64 L110 Y114 I343
Binding residue
(residue number reindexed from 1)		S13 L16 E17 C41 V42 V47 L93 Y97 I326
Annotation score2
Enzymatic activity
Catalytic site (original residue number in PDB) L54 C58 C63 K66 Y197 E201 A465 H467 E472
Catalytic site (residue number reindexed from 1) L37 C41 C46 K49 Y180 E184 A448 H450 E455
Enzyme Commision number 1.8.1.7: glutathione-disulfide reductase.
Gene Ontology
Molecular Function
GO:0004362 glutathione-disulfide reductase (NADPH) activity
GO:0016491 oxidoreductase activity
GO:0016668 oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
GO:0050660 flavin adenine dinucleotide binding
GO:0050661 NADP binding
Biological Process
GO:0006749 glutathione metabolic process
GO:0045454 cell redox homeostasis

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:4grt, PDBe:4grt, PDBj:4grt
PDBsum4grt
PubMed9174360
UniProtP00390|GSHR_HUMAN Glutathione reductase, mitochondrial (Gene Name=GSR)

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