› 2xi6

X-ray diffraction
1.65Å resolution

The structure of ascorbate peroxidase Compound I

Released:
DOI: 10.2210/pdb2xi6/pdb
PDB entry 2xi6 coloured by chain, front view.
PDB entry 2xi6 coloured by chain, side view.
PDB entry 2xi6 coloured by chain, top view.
Source organism: Glycine max
Primary publication:
Nature of the ferryl heme in compounds I and II.
Gumiero A, Metcalfe CL, Pearson AR, Raven EL, Moody PC
J Biol Chem 286 1260-8 (2011)
PMID: 21062738

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 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: 249 amino acids
Theoretical weight: 26.96 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
2 bound ligands:
Ligand SO4 2 x SO4
Ligand K 1 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P42212
Unit cell:
a: 82.03Å b: 82.03Å c: 75.19Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.148 0.176
Expression system: Escherichia coli

Quick links

Citations

11 review citations

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

3 mentions without citation

Nature of the ferryl heme in compounds I and II.
Gumiero et al. (2011)
2 more