Structure of PDB 4pv5 Chain B

Receptor sequence

>4pv5B (length=182) Species: 10090 (Mus musculus)

EPQPASSGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRV
LGLTLLQKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATLELT
HNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKK
PDDGKMKGLAFIQDPDGYWIEILNPNKIATII

3D structure

• PDB: 4pv5 Structural basis for 18-beta-glycyrrhetinic acid as a novel non-GSH analog glyoxalase I inhibitor
• Chain: B
• Resolution: 2.3 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Q34 E100 H127 E173
• Catalytic site (residue number reindexed from 1): Q32 E98 H125 E171
• 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	B	H127 E173	H125 E171
BS02	CBW	B	R38 N104	R36 N102	PDBbind-CN: -logKd/Ki=6.54,Ki=0.29uM
BS03	ZN	B	Q34 E100	Q32 E98

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:4pv5, PDBe:4pv5, PDBj:4pv5
• PDBsum: 4pv5
• PubMed: 26279158
• UniProt: Q9CPU0|LGUL_MOUSE Lactoylglutathione lyase (Gene Name=Glo1)