› 2vnz

X-ray diffraction
1.3Å resolution

Crystal structure of dithinonite reduced soybean ascorbate peroxidase mutant W41A.

Released:
DOI: 10.2210/pdb2vnz/pdb
PDB entry 2vnz coloured by chain, front view.
PDB entry 2vnz coloured by chain, side view.
PDB entry 2vnz coloured by chain, top view.
Source organism: Glycine max
Primary publication:
Iron oxidation state modulates active site structure in a heme peroxidase.
Badyal SK, Metcalfe CL, Basran J, Efimov I, Moody PC, Raven EL
Biochemistry 47 4403-9 (2008)
PMID: 18351739

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174998 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-ascorbate peroxidase Chain: X
Molecule details ›
Chain: X
Length: 261 amino acids
Theoretical weight: 28.25 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 NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P42212
Unit cell:
a: 81.78Å b: 81.78Å c: 75.244Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.182 0.181 0.199
Expression system: Escherichia coli

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Citations

1 review citation

Environmental heme-based sensor proteins: implications for understanding bacterial pathogenesis.
Farhana et al. (2012)
3 other articles