› 4usc

X-ray diffraction
2.6Å resolution

Crystal structure of peroxidase from palm tree Chamaerops excelsa

Released:
DOI: 10.2210/pdb4usc/pdb
PDB entry 4usc coloured by chain, front view.
PDB entry 4usc coloured by chain, side view.
PDB entry 4usc coloured by chain, top view.
Source organism: Trachycarpus fortunei
Primary publication:
Crystal structure analysis of peroxidase from the palm tree Chamaerops excelsa.
Bernardes A, Textor LC, Santos JC, Cuadrado NH, Kostetsky EY, Roig MG, Bavro VN, Muniz JR, Shnyrov VL, Polikarpov I
Biochimie 111 58-69 (2015)
PMID: 25660651

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-100797 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (3 distinct):
Peroxidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 303 amino acids
Theoretical weight: 31.96 KDa
Source organism: Trachycarpus fortunei
UniProt:
  • Canonical: A0A0A0Y4H8 (Residues: 22-324; Coverage: 94%)
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
Carbohydrate polymer : NEW Components: MAN, NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
7 bound ligands:
Ligand CA 4 x CA
Ligand MAN 1 x MAN
Ligand NAG 5 x NAG
Ligand SO4 2 x SO4
Ligand PEG 1 x PEG
Ligand EDO 2 x EDO
Ligand PEO 1 x PEO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LNLS BEAMLINE W01B-MX2
Spacegroup: P212121
Unit cell:
a: 70.18Å b: 100.65Å c: 132.31Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.218 0.246

Quick links

Citations

1 review citation

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