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Receptor Information

>5grt 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 ID

TS4

InChI

InChI=1S/C34H66N12O10S2/c35-11-1-3-13-39-15-5-17-41-29(49)19-43-31(51)25(45-27(47)9-7-23(37)33(53)54)21-57-58-22-26(46-28(48)10-8-24(38)34(55)56)32(52)44-20-30(50)42-18-6-16-40-14-4-2-12-36/h23-26,39-40H,1-22,35-38H2,(H,41,49)(H,42,50)(H,43,51)(H,44,52)(H,45,47)(H,46,48)(H,53,54)(H,55,56)/t23-,24-,25+,26+/m1/s1

InChIKey

HCMZDPYSWPSKSP-XPGKHFPBSA-N

SMILES

Software	SMILES
OpenEye OEToolkits 1.5.0	C(CCNCCCNC(=O)CNC(=O)C(CSSCC(C(=O)NCC(=O)NCCCNCCCCN)NC(=O)CCC(C(=O)O)N)NC(=O)CCC(C(=O)O)N)CN
CACTVS 3.341	NCCCCNCCCNC(=O)CNC(=O)[CH](CSSC[CH](NC(=O)CC[CH](N)C(O)=O)C(=O)NCC(=O)NCCCNCCCCN)NC(=O)CC[CH](N)C(O)=O
CACTVS 3.341	NCCCCNCCCNC(=O)CNC(=O)[C@H](CSSC[C@H](NC(=O)CC[C@@H](N)C(O)=O)C(=O)NCC(=O)NCCCNCCCCN)NC(=O)CC[C@@H](N)C(O)=O
OpenEye OEToolkits 1.5.0	C(CCNCCCNC(=O)CNC(=O)[C@H](CSSC[C@@H](C(=O)NCC(=O)NCCCNCCCCN)NC(=O)CC[C@H](C(=O)O)N)NC(=O)CC[C@H](C(=O)O)N)CN
ACDLabs 10.04	O=C(NC(C(=O)NCC(=O)NCCCNCCCCN)CSSCC(C(=O)NCC(=O)NCCCNCCCCN)NC(=O)CCC(C(=O)O)N)CCC(C(=O)O)N

Formula

C34 H66 N12 O10 S2

Name

GLUTATHIONYLSPERMIDINE DISULFIDE

PDB chain

5grt Chain A Residue 17 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]

Receptor-Ligand Complex Structure

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Structure summary

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PDB	5grt Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity.
Resolution	2.4 Å
Binding residue (original residue number in PDB)	S30 E34 C58 V59 Y106 L110 I113 Y114 T339 I343
Binding residue (residue number reindexed from 1)	S13 E17 C41 V42 Y89 L93 I96 Y97 T322 I326
Annotation score	2

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.

	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

PDB	RCSB:5grt, PDBe:5grt, PDBj:5grt
PDBsum	5grt
PubMed	9174360
UniProt	P00390\|GSHR_HUMAN Glutathione reductase, mitochondrial (Gene Name=GSR)

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Structure of PDB 5grt Chain A Binding Site BS02