Structure of PDB 1grt Chain A

Receptor sequence
>1grtA (length=462) Species: 9606 (Homo sapiens) [Search protein sequence]
AVASYDYLVIGGGSGGLESAWRAAELGARAAVVESHKLGGTCVNVGCVPK
KVMWNTAVHSEFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQN
NLTKSHIEIIRGHAAFTSDPKPTIEVSGKKYTAPHILIATGGMPSTPHES
QIPGASLGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLM
IRHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTLSGLEVSMV
TAVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVD
EFQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNN
IPTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTK
CVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAI
HPTSSEELVTLR
3D structure
PDB1grt Glutathione reductase turned into trypanothione reductase: structural analysis of an engineered change in substrate specificity.
ChainA
Resolution2.3 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) L38 C42 C47 K50 Y181 E185 A449 H451 E456
Enzyme Commision number 1.8.1.7: glutathione-disulfide reductase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 FAD A G27 G29 S30 G31 E50 S51 G56 T57 C58 G62 C63 K66 A130 T156 G157 Y197 G330 D331 L337 L338 T339 G11 G13 S14 G15 E34 S35 G40 T41 C42 G46 C47 K50 A114 T140 G141 Y181 G314 D315 L321 L322 T323
Gene Ontology
Molecular Function
GO:0004362 glutathione-disulfide reductase (NADPH) activity
GO:0009055 electron transfer 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:0034599 cellular response to oxidative stress
GO:0045454 cell redox homeostasis
GO:0098869 cellular oxidant detoxification
Cellular Component
GO:0005737 cytoplasm
GO:0005739 mitochondrion
GO:0005759 mitochondrial matrix
GO:0005829 cytosol
GO:0009897 external side of plasma membrane
GO:0070062 extracellular exosome

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1grt, PDBe:1grt, PDBj:1grt
PDBsum1grt
PubMed9174360
UniProtP00390|GSHR_HUMAN Glutathione reductase, mitochondrial (Gene Name=GSR)

[Back to BioLiP]