Structure of PDB 4g0l Chain A

Receptor sequence
>4g0lA (length=327) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
GQLIDGVWHDTWYDTKSTGGKFQRSASAFRNWLTADGAPGPTGTGGFIAE
KDRYHLYVSLACPWAHRTLIMRKLKGLEPFISVSVVNPLMLENGWTFDDS
FPGATGDTLYQNEFLYQLYLHADPHYSGRVTVPVLWDKKNHTIVSNESAE
IIRMFNTAFDALGAKAGDYYPPALQTKIDELNGWIYDTVNNGVYKAGFAT
SQEAYDEAVAKVFESLARLEQILGQHRYLTGNQLTEADIRLWTTLVRFDP
VYVTHFKCDKHRISDYLNLYGFLRDIYQMPGIAETVNFDHIRNHYFRSHK
TINPTGIISIGPWQDLDEPHGRDVRFG
3D structure
PDB4g0l Structural understanding of the glutathione-dependent reduction mechanism of glutathionyl-hydroquinone reductases.
ChainA
Resolution2.62 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 1.8.5.7: glutathionyl-hydroquinone 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 GSH A C63 W65 W96 R130 T132 V133 E148 S149 C62 W64 W95 R129 T131 V132 E147 S148 PDBbind-CN: -logKd/Ki=5.19,Kd=6.5uM
Gene Ontology
Molecular Function
GO:0004364 glutathione transferase activity
GO:0016491 oxidoreductase activity
GO:0016672 oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor
GO:0042803 protein homodimerization activity
Cellular Component
GO:0005737 cytoplasm

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Molecular Function
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Cellular Component
External links
PDB RCSB:4g0l, PDBe:4g0l, PDBj:4g0l
PDBsum4g0l
PubMed22955277
UniProtP42620|YQJG_ECOLI Glutathionyl-hydroquinone reductase YqjG (Gene Name=yqjG)

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