› 1qh5

X-ray diffraction
1.45Å resolution

HUMAN GLYOXALASE II WITH S-(N-HYDROXY-N-BROMOPHENYLCARBAMOYL)GLUTATHIONE

Released:
DOI: 10.2210/pdb1qh5/pdb
PDB entry 1qh5 coloured by chain, front view.
PDB entry 1qh5 coloured by chain, side view.
PDB entry 1qh5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue.
Cameron AD, Ridderström M, Olin B, Mannervik B
Structure 7 1067-78 (1999)
PMID: 10508780

Function and Biology Details

Reaction catalysed: 
S-(2-hydroxyacyl)glutathione + H(2)O = glutathione + a 2-hydroxy carboxylate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172576 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hydroxyacylglutathione hydrolase, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 260 amino acids
Theoretical weight: 28.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16775 (Residues: 49-308; Coverage: 84%)
Gene names: GLO2, HAGH, HAGH1
Sequence domains:
Structure domains: Ribonuclease Z/Hydroxyacylglutathione hydrolase-like

Ligands and Environments


Cofactor: Ligand GSH 1 x GSH

Cofactor: Ligand GBP 1 x GBP
1 bound ligand:
Ligand ZN 4 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 39.55Å b: 73.8Å c: 164.7Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.232
Expression system: Escherichia coli

Quick links

Citations

24 review citations

Acinetobacter baumannii: emergence of a successful pathogen.
Peleg et al. (2008)
23 more

28 mentions without citation

Thioesterases: a new perspective based on their primary and tertiary structures.
Cantu et al. (2010)
27 more