Structure of PDB 4opn Chain A

Receptor sequence

>4opnA (length=172) Species: 10090 (Mus musculus)

SGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLL
QKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATLELTHNWGTE
DDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKM
KGLAFIQDPDGYWIEILNPNKI

3D structure

• PDB: 4opn Reversible Inhibition of Glyoxalase I: Synthesis and Activity Evaluation
• Chain: A
• Resolution: 2.1 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Q34 E100 H127 E173
• Catalytic site (residue number reindexed from 1): Q26 E92 H119 E165
• 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	Q34 E100	Q26 E92
BS02	ZBF	A	R123 H127 K151 K157 M158 L161 E173 I180	R115 H119 K143 K149 M150 L153 E165 I172
BS03	ZBF	A	Q34 R38 F68 F93 E100 T102 N104	Q26 R30 F60 F85 E92 T94 N96

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:4opn, PDBe:4opn, PDBj:4opn
• PDBsum: 4opn
• UniProt: Q9CPU0|LGUL_MOUSE Lactoylglutathione lyase (Gene Name=Glo1)