Structure of PDB 1fa6 Chain B Binding Site BS01
Receptor Information
>1fa6 Chain B (length=128) Species:
562
(Escherichia coli) [
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MRLLHTMLRVGDLQRSIDFYTKVLGMKLLRTSENPEYKYSLAFVGYGPET
EEAVIELTYNWGVDKYELGTAYGHIALSVDNAAEACEKIRQNGGNVTREA
GPVKGGTTVIAFVEDPDGYKIELIEEGN
Ligand information
Ligand ID
CO
InChI
InChI=1S/Co/q+2
InChIKey
XLJKHNWPARRRJB-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Co+2]
CACTVS 3.341
[Co++]
Formula
Co
Name
COBALT (II) ION
ChEMBL
DrugBank
DB14205
ZINC
PDB chain
1fa6 Chain A Residue 1200 [
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Receptor-Ligand Complex Structure
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PDB
1fa6
Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation.
Resolution
1.9 Å
Binding residue
(original residue number in PDB)
H74 E122
Binding residue
(residue number reindexed from 1)
H74 E122
Annotation score
1
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.
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:1fa6
,
PDBe:1fa6
,
PDBj:1fa6
PDBsum
1fa6
PubMed
10913283
UniProt
P0AC81
|LGUL_ECOLI Lactoylglutathione lyase (Gene Name=gloA)
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