Structure of PDB 6s0i Chain A

Receptor sequence
>6s0iA (length=251) Species: 83333 (Escherichia coli K-12) [Search protein sequence]
MNLNSIPAFDDNYIWVLNDEAGRCLIVDPGDAEPVLNAIAANNWQPEAIF
LTHHHHDHVGGVKELVEKFPQIVVYGPQETQDKGTTQVVKDGETAFVLGH
EFSVIATPGHTLGHICYFSKPYLFCGDTLFSGGCGRLFEGTASQMYQSLK
KLSALPDDTLVCCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQ
ITLPVILKNERQINVFLRTEDIDLINVINEETLLQQPEERFAWLRSKKDR
F
3D structure
PDB6s0i Crystal structure of Escherichia coli Glyoxalase II
ChainA
Resolution1.803 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H53 H55 D57 H58 H110 D127 H165
Catalytic site (residue number reindexed from 1) H53 H55 D57 H58 H110 D127 H165
Enzyme Commision number 3.1.2.6: hydroxyacylglutathione hydrolase.
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 ZN A H58 D127 H165 H58 D127 H165
BS02 ZN A H53 H55 H110 D127 H53 H55 H110 D127
Gene Ontology
Molecular Function
GO:0004416 hydroxyacylglutathione hydrolase activity
GO:0008270 zinc ion binding
GO:0016787 hydrolase activity
GO:0046872 metal ion binding
Biological Process
GO:0009408 response to heat
GO:0009636 response to toxic substance
GO:0019243 methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione

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Molecular Function
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Biological Process
External links
PDB RCSB:6s0i, PDBe:6s0i, PDBj:6s0i
PDBsum6s0i
PubMed
UniProtP0AC84|GLO2_ECOLI Hydroxyacylglutathione hydrolase GloB (Gene Name=gloB)

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