Structure of PDB 4kyk Chain A Binding Site BS01

Receptor Information

>4kyk Chain A (length=179) Species: 10090 (Mus musculus)

PASSGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGL
TLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATLELTHNW
GTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDD
GKMKGLAFIQDPDGYWIEILNPNKIATII

Ligand information

• Ligand ID: ZN
• InChI: InChI=1S/Zn/q+2
• InChIKey: PTFCDOFLOPIGGS-UHFFFAOYSA-N
• SMILES:
  CACTVS 3.341: [Zn++]
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Zn+2]
• Formula: Zn
• Name: ZINC ION
• ChEMBL: CHEMBL1236970
• DrugBank: DB14532
• PDB chain: 4kyk Chain A Residue 201

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4kyk Zopolrestat as a human glyoxalase I inhibitor and its structural basis.
• Resolution: 2.0 Å
• Binding residue (original residue number in PDB): H127 E173
• Binding residue (residue number reindexed from 1): H122 E168
• Annotation score: 1

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.

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

External links

• PDB: RCSB:4kyk, PDBe:4kyk, PDBj:4kyk
• PDBsum: 4kyk
• PubMed: 23857942
• UniProt: Q9CPU0|LGUL_MOUSE Lactoylglutathione lyase (Gene Name=Glo1)