› 1v0h

X-ray diffraction
1.46Å resolution

ASCOBATE PEROXIDASE FROM SOYBEAN CYTOSOL IN COMPLEX WITH SALICYLHYDROXAMIC ACID

Released:
DOI: 10.2210/pdb1v0h/pdb
PDB entry 1v0h coloured by chain, front view.
PDB entry 1v0h coloured by chain, side view.
PDB entry 1v0h coloured by chain, top view.
Source organism: Glycine max
Primary publication:
Crystal structure of the ascorbate peroxidase-salicylhydroxamic acid complex.
Sharp KH, Moody PC, Brown KA, Raven EL
Biochemistry 43 8644-51 (2004)
PMID: 15236572

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: X
Molecule details ›
Chain: X
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
2 bound ligands:
Ligand NA 1 x NA
Ligand SHA 1 x SHA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P42212
Unit cell:
a: 82.77Å b: 82.77Å c: 74.991Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.151 0.15 0.182
Expression system: Escherichia coli

Quick links

Citations

24 citation in other articles

Directed evolution of APEX2 for electron microscopy and proximity labeling.
Lam et al. (2015)
23 more

5 mentions without citation

Engineered ascorbate peroxidase as a genetically encoded reporter for electron microscopy.
Martell et al. (2012)
4 more