› 3zch

X-ray diffraction
2Å resolution

Ascorbate peroxidase W41A-H42M mutant

Released:
DOI: 10.2210/pdb3zch/pdb
PDB entry 3zch coloured by chain, front view.
PDB entry 3zch coloured by chain, side view.
PDB entry 3zch coloured by chain, top view.
Source organism: Glycine max
Primary publication:
Probing the conformational mobility of the active site of a heme peroxidase.
Gumiero A, Guimero A, Badyal SK, Leeks T, Moody PC, Raven EL
Dalton Trans 42 3170-5 (2013)
PMID: 23202589

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: A
Molecule details ›
Chain: A
Length: 261 amino acids
Theoretical weight: 28.24 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
3 bound ligands:
Ligand SO4 2 x SO4
Ligand EPE 2 x EPE
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: 82.629Å b: 82.629Å c: 74.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.153 0.198
Expression system: Escherichia coli

Quick links

Citations

1 mention without citation

In silico characterization and homology modeling of cytosolic APX gene predicts novel glycine residue modulating waterlogging stress response in pigeon pea.
Tyagi et al. (2021)