Structure of PDB 1fro Chain B

Receptor sequence

>1froB (length=176) Species: 9606 (Homo sapiens)

GGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLI
QKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTE
DDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKM
KGLAFIQDPDGYWIEILNPNKMATLM

3D structure

• PDB: 1fro Crystal structure of human glyoxalase I--evidence for gene duplication and 3D domain swapping.
• Chain: B
• Resolution: 2.2 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): Q33 E99 H126 E172
• 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	Q33 E99	Q26 E92
BS02	GSB	B	R37 F67 T101 N103	R30 F60 T94 N96
BS03	ZN	B	H126 E172	H119 E165
BS04	GSB	B	R122 M157 F162 E172 M183	R115 M150 F155 E165 M176

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:1fro, PDBe:1fro, PDBj:1fro
• PDBsum: 1fro
• PubMed: 9218781
• UniProt: Q04760|LGUL_HUMAN Lactoylglutathione lyase (Gene Name=GLO1)