› 1al8

X-ray diffraction
2.2Å resolution

THREE-DIMENSIONAL STRUCTURE OF GLYCOLATE OXIDASE WITH BOUND ACTIVE-SITE INHIBITORS

Released:
DOI: 10.2210/pdb1al8/pdb
PDB entry 1al8 coloured by chain, front view.
PDB entry 1al8 coloured by chain, side view.
PDB entry 1al8 coloured by chain, top view.
Source organism: Spinacia oleracea
Primary publication:
Three-dimensional structures of glycolate oxidase with bound active-site inhibitors.
Stenberg K, Lindqvist Y
Protein Sci 6 1009-15 (1997)
PMID: 9144771

Function and Biology Details

Reaction catalysed: 
(S)-2-hydroxy acid + O(2) = 2-oxo acid + H(2)O(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138662 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycolate oxidase Chain: A
Molecule details ›
Chain: A
Length: 359 amino acids
Theoretical weight: 39.34 KDa
Source organism: Spinacia oleracea
Expression system: Escherichia coli
UniProt:
  • Canonical: P05414 (Residues: 1-359; Coverage: 97%)
Sequence domains: FMN-dependent dehydrogenase
Structure domains: Aldolase class I

Ligands and Environments


Cofactor: Ligand FMN 1 x FMN
1 bound ligand:
Ligand DHP 1 x DHP
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I4
Unit cell:
a: 95.4Å b: 95.4Å c: 93.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.251
Expression system: Escherichia coli

Quick links

Citations

7 review citations

To be or not to be an oxidase: challenging the oxygen reactivity of flavoenzymes.
Mattevi A. (2006)
6 more

4 mentions without citation

Coupling between catalytic site and collective dynamics: a requirement for mechanochemical activity of enzymes.
Yang et al. (2005)
3 more