Structure of PDB 1bh5 Chain A

Receptor sequence

>1bh5A (length=177) Species: 9606 (Homo sapiens)

SGGLTDEAALSCCSDADPSTKDFLLQETMLRVKDPKKSLDFYTRVLGMTL
IQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGT
EDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGK
MKGLAFIQDPDGYWIQILNPNKMATLM

3D structure

• PDB: 1bh5 Involvement of an active-site Zn2+ ligand in the catalytic mechanism of human glyoxalase I.
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E33 E99 H126 Q172
• Catalytic site (residue number reindexed from 1): E27 E93 H120 Q166
• 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	H126 Q172	H120 Q166
BS02	GTX	A	R122 M157 F162	R116 M151 F156
BS03	ZN	A	E33 E99	E27 E93
BS04	GTX	A	R37 F67 L69 T101 N103	R31 F61 L63 T95 N97

Gene Ontology

Molecular Function

• GO:0004462 lactoylglutathione lyase activity
• GO:0005515 protein binding
• GO:0008270 zinc ion binding
• GO:0016829 lyase activity
• GO:0046872 metal ion binding

Biological Process

• GO:0005975 carbohydrate metabolic process
• GO:0006357 regulation of transcription by RNA polymerase II
• GO:0006749 glutathione metabolic process
• GO:0009438 methylglyoxal metabolic process
• GO:0030316 osteoclast differentiation
• GO:0043066 negative regulation of apoptotic process

Cellular Component

• GO:0005654 nucleoplasm
• GO:0005737 cytoplasm
• GO:0005829 cytosol
• GO:0005886 plasma membrane
• GO:0070062 extracellular exosome

External links

• PDB: RCSB:1bh5, PDBe:1bh5, PDBj:1bh5
• PDBsum: 1bh5
• PubMed: 9705294
• UniProt: Q04760|LGUL_HUMAN Lactoylglutathione lyase (Gene Name=GLO1)