PDBe 1apx

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURE OF RECOMBINANT ASCORBATE PEROXIDASE

Released:
Source organism: Pisum sativum
Primary publication:
Crystal structure of recombinant pea cytosolic ascorbate peroxidase.
Biochemistry 34 4331-41 (1995)
PMID: 7703247

Function and Biology Details

Reaction catalysed:
2 L-ascorbate + H(2)O(2) + 2 H(+) = L-ascorbate + L-dehydroascorbate + 2 H(2)O. 
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-ascorbate peroxidase, cytosolic Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 249 amino acids
Theoretical weight: 27.1 KDa
Source organism: Pisum sativum
Expression system: Escherichia coli
UniProt:
  • Canonical: P48534 (Residues: 2-250; Coverage: 100%)
Gene names: APPX1, APX1
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 132.4Å b: 53Å c: 170.6Å
α: 90° β: 107.1° γ: 90°
R-values:
R R work R free
0.193 0.193 not available
Expression system: Escherichia coli