Structure of PDB 4grt Chain A

Receptor sequence
>4grtA (length=461) Species: 9606 (Homo sapiens) [Search protein sequence]
VASYDYLVIGGGSGGLESAWRAAELGARAAVVESHKLGGTCVNVGCVPKK
VMWNTAVHSEFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNN
LTKSHIEIIRGHAAFTSDPKPTIEVSGKKYTAPHILIATGGMPSTPHESQ
IPGASLGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMI
RHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTLSGLEVSMVT
AVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDE
FQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNI
PTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKC
VMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIH
PTSSEELVTLR
3D structure
PDB4grt Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity.
ChainA
Resolution2.8 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
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.
Interaction with ligand
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)

[Back to BioLiP]