› 4cuo

X-ray diffraction
1.67Å resolution

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-100598 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Peroxidase Chain: A
Molecule details ›
Chain: A
Length: 306 amino acids
Theoretical weight: 32.98 KDa
Source organism: Ficus benghalensis
UniProt:
  • Canonical: A0A087WNH2 (Residues: 1-306; Coverage: 100%)
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC, BMA, XYS, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
6 bound ligands:
Ligand NAG 3 x NAG
Ligand CA 2 x CA
Ligand NA 1 x NA
Ligand CL 3 x CL
Ligand SO4 3 x SO4
Ligand CO3 4 x CO3
1 modified residue:
Ligand SNN 1 x SNN

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X12
Spacegroup: P3221
Unit cell:
a: 73.115Å b: 73.115Å c: 164.596Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.158 0.157 0.18

Quick links

Citations

1 review citation

Phenoloxidases in Plants-How Structural Diversity Enables Functional Specificity.
Blaschek et al. (2021)
3 other articles

2 mentions without citation

Post-translational modification and extended glycosylation pattern of a plant latex peroxidase of native source characterized by X-ray crystallography.
Palm et al. (2014)
1 more