Structure of PDB 4g0l Chain B

Receptor sequence
>4g0lB (length=326) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
QLIDGVWHDTWYDTKSTGGKFQRSASAFRNWLTADGAPGPTGTGGFIAEK
DRYHLYVSLACPWAHRTLIMRKLKGLEPFISVSVVNPLMLENGWTFDDSF
PGATGDTLYQNEFLYQLYLHADPHYSGRVTVPVLWDKKNHTIVSNESAEI
IRMFNTAFDALGAKAGDYYPPALQTKIDELNGWIYDTVNNGVYKAGFATS
QEAYDEAVAKVFESLARLEQILGQHRYLTGNQLTEADIRLWTTLVRFDPV
YVTHFKCDKHRISDYLNLYGFLRDIYQMPGIAETVNFDHIRNHYFRSHKT
INPTGIISIGPWQDLDEPHGRDVRFG
3D structure
PDB4g0l Structural understanding of the glutathione-dependent reduction mechanism of glutathionyl-hydroquinone reductases.
ChainB
Resolution2.62 Å
3D
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
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 B C63 W65 W96 R130 T132 V133 E148 S149 C61 W63 W94 R128 T130 V131 E146 S147
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

View graph for
Molecular Function

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

[Back to BioLiP]