› 1oag

X-ray diffraction
1.75Å resolution

Ascorbate peroxidase from soybean cytosol

Released:
DOI: 10.2210/pdb1oag/pdb
PDB entry 1oag coloured by chain, front view.
PDB entry 1oag coloured by chain, side view.
PDB entry 1oag coloured by chain, top view.
Source organism: Glycine max
Primary publication:
Crystal structure of the ascorbate peroxidase-ascorbate complex.
Sharp KH, Mewies M, Moody PC, Raven EL
Nat Struct Biol 10 303-7 (2003)
PMID: 12640445

Function and Biology Details

Reaction catalysed: 
(1a) 2 L-ascorbate + H(2)O(2) + 2 H(+) = 2 monodehydroascorbate + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-559331 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-ascorbate peroxidase Chain: A
Molecule details ›
Chain: A
Length: 261 amino acids
Theoretical weight: 28.36 KDa
Source organism: Glycine max
Expression system: Escherichia coli
UniProt:
  • Canonical: Q43758 (Residues: 2-250; Coverage: 100%)
Gene name: apx1
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P42212
Unit cell:
a: 81.842Å b: 81.842Å c: 75.031Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.144 0.142 0.177
Expression system: Escherichia coli

Quick links

Citations

14 review citations

Heme enzyme structure and function.
Poulos TL. (2014)
13 more

10 mentions without citation

Proximity Dependent Biotinylation: Key Enzymes and Adaptation to Proteomics Approaches.
Samavarchi-Tehrani et al. (2020)
9 more