› 5jqr

X-ray diffraction
1.81Å resolution

The Structure of Ascorbate Peroxidase Compound II formed by reaction with m-CPBA

Released:
DOI: 10.2210/pdb5jqr/pdb
PDB entry 5jqr coloured by chain, front view.
PDB entry 5jqr coloured by chain, side view.
PDB entry 5jqr coloured by chain, top view.
Source organism: Glycine max
Primary publication:
Direct visualization of a Fe(IV)-OH intermediate in a heme enzyme.
Kwon H, Basran J, Casadei CM, Fielding AJ, Schrader TE, Ostermann A, Devos JM, Aller P, Blakeley MP, Moody PCE, Raven EL
OpenAccess logo Nat Commun 7 13445 (2016)
PMID: 27897163

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: 249 amino acids
Theoretical weight: 26.96 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 K 1 x K
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P42212
Unit cell:
a: 82.095Å b: 82.095Å c: 75.162Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.157 0.154 0.214
Expression system: Escherichia coli

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Citations

7 review citations

Oxygen Activation and Radical Transformations in Heme Proteins and Metalloporphyrins.
Huang et al. (2018)
6 more

3 mentions without citation

Direct visualization of a Fe(IV)-OH intermediate in a heme enzyme.
Kwon et al. (2016)
2 more