Structure of PDB 4kyk Chain A

Receptor sequence
>4kykA (length=179) Species: 10090 (Mus musculus) [Search protein sequence]
PASSGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGL
TLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATLELTHNW
GTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDD
GKMKGLAFIQDPDGYWIEILNPNKIATII
3D structure
PDB4kyk Zopolrestat as a human glyoxalase I inhibitor and its structural basis.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Q34 E100 H127 E173
Catalytic site (residue number reindexed from 1) Q29 E95 H122 E168
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 H127 E173 H122 E168
BS02 ZN A Q34 E100 Q29 E95
Gene Ontology
Molecular Function
GO:0004462 lactoylglutathione lyase activity
GO:0008270 zinc ion binding
GO:0016829 lyase activity
GO:0046872 metal ion binding
Biological Process
GO:0006357 regulation of transcription by RNA polymerase II
GO:0006749 glutathione metabolic process
GO:0009438 methylglyoxal metabolic process
GO:0019243 methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione
GO:0030316 osteoclast differentiation
GO:0043066 negative regulation of apoptotic process
Cellular Component
GO:0005654 nucleoplasm
GO:0005829 cytosol
GO:0005886 plasma membrane

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Molecular Function
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Cellular Component
External links
PDB RCSB:4kyk, PDBe:4kyk, PDBj:4kyk
PDBsum4kyk
PubMed23857942
UniProtQ9CPU0|LGUL_MOUSE Lactoylglutathione lyase (Gene Name=Glo1)

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