Structure of PDB 1fa5 Chain A

Receptor sequence
>1fa5A (length=128) Species: 562 (Escherichia coli) [Search protein sequence]
MRLLHTMLRVGDLQRSIDFYTKVLGMKLLRTSENPEYKYSLAFVGYGPET
EEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACEKIRQNGGNVTREA
GPVKGGTTVIAFVEDPDGYKIELIEEGN
3D structure
PDB1fa5 Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation.
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H5 E56 H74 E122
Catalytic site (residue number reindexed from 1) H5 E56 H74 E122
Enzyme Commision number 4.4.1.5: lactoylglutathione lyase.
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 H5 E56 H5 E56
BS02 ZN A H74 E122 H74 E122
Gene Ontology
Molecular Function
GO:0004462 lactoylglutathione lyase activity
GO:0005515 protein binding
GO:0016151 nickel cation binding
GO:0016829 lyase activity
GO:0042803 protein homodimerization activity
GO:0046872 metal ion binding
Biological Process
GO:0009636 response to toxic substance
GO:0019243 methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione
Cellular Component
GO:0005737 cytoplasm
GO:0005829 cytosol

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1fa5, PDBe:1fa5, PDBj:1fa5
PDBsum1fa5
PubMed10913283
UniProtP0AC81|LGUL_ECOLI Lactoylglutathione lyase (Gene Name=gloA)

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