› 2rdt

X-ray diffraction
1.95Å resolution

Crystal Structure of Human Glycolate Oxidase (GO) in Complex with CDST

Released:
DOI: 10.2210/pdb2rdt/pdb
PDB entry 2rdt coloured by chain, front view.
PDB entry 2rdt coloured by chain, side view.
PDB entry 2rdt coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design.
Murray MS, Holmes RP, Lowther WT
Biochemistry 47 2439-49 (2008)
PMID: 18215067

Function and Biology Details

Reactions catalysed: 
(S)-2-hydroxy acid + O(2) = 2-oxo acid + H(2)O(2)
Glyoxylate + H(2)O + O(2) = oxalate + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193816 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-Hydroxyacid oxidase 1 Chain: A
Molecule details ›
Chain: A
Length: 387 amino acids
Theoretical weight: 42.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UJM8 (Residues: 1-370; Coverage: 100%)
Gene names: GOX1, HAO1
Sequence domains: FMN-dependent dehydrogenase
Structure domains: Aldolase class I

Ligands and Environments


Cofactor: Ligand FMN 1 x FMN
1 bound ligand:
Ligand 2RD 1 x 2RD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: I4
Unit cell:
a: 96.322Å b: 96.322Å c: 79.194Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.177 0.223
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Molecular basis of primary hyperoxaluria: clues to innovative treatments.
Dindo et al. (2019)
3 more

4 mentions without citation

Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design.
Murray et al. (2008)
3 more