› 7s10

X-ray diffraction
1.4Å resolution

Crystal Structure of ascorbate peroxidase triple mutant: S160M, L203M, Q204M

Released:
DOI: 10.2210/pdb7s10/pdb
PDB entry 7s10 coloured by chain, front view.
PDB entry 7s10 coloured by chain, side view.
PDB entry 7s10 coloured by chain, top view.
Source organism: Glycine max
Primary publication:
Computational analysis of the tryptophan cation radical energetics in peroxidase Compound I.
Poulos TL, Kim JS, Murarka VC
OpenAccess logo J Biol Inorg Chem 27 229-237 (2022)
PMID: 35064363

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:
  • not assigned
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: 248 amino acids
Theoretical weight: 26.95 KDa
Source organism: Glycine max
Expression system: Escherichia coli
UniProt:
  • Canonical: Q43758 (Residues: 2-249; Coverage: 99%)
Gene name: apx1
Sequence domains: Peroxidase

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: SSRL BEAMLINE BL12-2
Spacegroup: P42212
Unit cell:
a: 82.644Å b: 82.644Å c: 75.322Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.171 0.208
Expression system: Escherichia coli

Quick links

Citations

1 mention without citation

Computational analysis of the tryptophan cation radical energetics in peroxidase Compound I.
Poulos et al. (2022)