Structure of PDB 1k4q Chain A

Receptor sequence
>1k4qA (length=461) Species: 9606 (Homo sapiens) [Search protein sequence]
VASYDYLVIGGGSGGLASARRAAELGARAAVVESHKLGGTCVNVGCVPKK
VMWNTAVHSEFMHDHADYGFPSCEGKFNWRVIKEKRDAYVSRLNAIYQNN
LTKSHIEIIRGHAAFTSDPKPTIEVSGKKYTAPHILIATGGMPSTPHESQ
IPGASLGITSDGFFQLEELPGRSVIVGAGYIAVEMAGILSALGSKTSLMI
RHDKVLRSFDSMISTNCTEELENAGVEVLKFSQVKEVKKTLSGLEVSMVT
AVPGRLPVMTMIPDVDCLLWAIGRVPNTKDLSLNKLGIQTDDKGHIIVDE
FQNTNVKGIYAVGDVCGKALLTPVAIAAGRKLAHRLFEYKEDSKLDYNNI
PTVVFSHPPIGTVGLTEDEAIHKYGIENVKTYSTSFTPMYHAVTKRKTKC
VMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGATKADFDNTVAIH
PTSSEELVTLR
3D structure
PDB1k4q Crystal structure of the antioxidant enzyme glutathione reductase inactivated by peroxynitrite.
ChainA
Resolution1.9 Å
3D
structure
Catalytic site residues are labeled in the structure
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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
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 S30 G31 E50 S51 G56 T57 C58 G62 C63 K66 H129 A130 T156 G157 Y197 R291 G330 D331 L337 L338 T339 S13 G14 E33 S34 G39 T40 C41 G45 C46 K49 H112 A113 T139 G140 Y180 R274 G313 D314 L320 L321 T322
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

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Molecular Function
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Biological Process
External links
PDB RCSB:1k4q, PDBe:1k4q, PDBj:1k4q
PDBsum1k4q
PubMed11705998
UniProtP00390|GSHR_HUMAN Glutathione reductase, mitochondrial (Gene Name=GSR)

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