4a5g

X-ray diffraction
2.05Å resolution

Raphanus sativus anionic peroxidase.

Released:
Source organism: Raphanus sativus
Entry authors: Jimenez-Arroyo N, Valderrama B, Gil-Rodriguez P, Rojas-Trejo SP, Rudino-Pinera E

Function and Biology Details

Reaction catalysed:
2 phenolic donor + H(2)O(2) = 2 phenoxyl radical of the donor + 2 H(2)O
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-125592 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (9 distinct):
Peroxidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 308 amino acids
Theoretical weight: 31.97 KDa
Source organism: Raphanus sativus
UniProt:
  • Canonical: K7N5L9 (Residues: 1-308; Coverage: 100%)
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
Carbohydrate polymer : NEW Components: NAG, BMA, XYP, MAN, FUC
Carbohydrate polymer : NEW Components: NAG, BMA, FUC
Carbohydrate polymer : NEW Components: NAG, MAN, FUL
Carbohydrate polymer : NEW Components: NAG, MAN, FUC
Carbohydrate polymer : NEW Components: NAG, BMA, XYP, FUL
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer : NEW Components: NAG, BMA, FUL
Carbohydrate polymer : NEW Components: NAG, FUC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: P21
Unit cell:
a: 59.148Å b: 41.192Å c: 137.796Å
α: 90° β: 96.91° γ: 90°
R-values:
R R work R free
0.164 0.163 0.185