› 1oaf

X-ray diffraction
1.4Å resolution

Ascobate peroxidase from soybean cytosol in complex with ascorbate

Released:
DOI: 10.2210/pdb1oaf/pdb
PDB entry 1oaf coloured by chain, front view.
PDB entry 1oaf coloured by chain, side view.
PDB entry 1oaf 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:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174997 (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

Cofactor: Ligand ASC 1 x ASC
1 bound ligand:
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P42212
Unit cell:
a: 81.328Å b: 81.328Å c: 74.884Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.161 0.196
Expression system: Escherichia coli

Quick links

Citations

14 review citations

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

14 mentions without citation

Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins.
Huang et al. (2018)
13 more