Structure of PDB 2za0 Chain B

Receptor sequence

>2za0B (length=176) Species: 10090 (Mus musculus)

SGLTDETAFSCCSDPDPSTKDFLLQQTMLRIKDPKKSLDFYTRVLGLTLL
QKLDFPAMKFSLYFLAYEDKNDIPKDKSEKTAWTFSRKATLELTHNWGTE
DDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKM
KGLAFIQDPDGYWIEILNPNKIATII

3D structure

• PDB: 2za0 The identification of an osteoclastogenesis inhibitor through the inhibition of glyoxalase I
• Chain: B
• Resolution: 1.7 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	B	Q34 E100	Q26 E92
BS02	ZN	B	H127 E173	H119 E165
BS03	MGI	B	Q34 M66 L70 E100	Q26 M58 L62 E92	PDBbind-CN: -logKd/Ki=6.64,Ki=0.23uM
BS04	MGI	B	H127 E173	H119 E165	PDBbind-CN: -logKd/Ki=6.64,Ki=0.23uM

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:2za0, PDBe:2za0, PDBj:2za0
• PDBsum: 2za0
• PubMed: 18695250
• UniProt: Q9CPU0|LGUL_MOUSE Lactoylglutathione lyase (Gene Name=Glo1)