› 2c1v

X-ray diffraction
1.2Å resolution

CRYSTAL STRUCTURE OF THE DI-HAEM CYTOCHROME C PEROXIDASE FROM PARACOCCUS PANTOTROPHUS - Mixed VALENCE FORM

Released:
DOI: 10.2210/pdb2c1v/pdb
Model geometry
Fit model/data
Data not analysed
PDB entry 2c1v coloured by chain, front view.
PDB entry 2c1v coloured by chain, side view.
PDB entry 2c1v coloured by chain, top view.
Source organism: Paracoccus pantotrophus
Primary publication:
Activation and catalysis of the di-heme cytochrome c peroxidase from Paracoccus pantotrophus.
Echalier A, Goodhew CF, Pettigrew GW, Fülöp V
Structure 14 107-17 (2006)
PMID: 16407070

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162656 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DI-HAEM CYTOCHROME C PEROXIDASE Chains: A, B
Molecule details ›
Chains: A, B
Length: 338 amino acids
Theoretical weight: 36.33 KDa
Source organism: Paracoccus pantotrophus
Structure domains: Cytochrome c-like domain

Ligands and Environments

3 bound ligands:
Ligand HEC 4 x HEC
Ligand CA 2 x CA
Ligand EDO 4 x EDO
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P21212
Unit cell:
a: 101.37Å b: 141.2Å c: 51.58Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.173 0.188

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Citations

11 review citations

Heme enzyme structure and function.
Poulos TL. (2014)
10 more

2 mentions without citation

Heterolytic OO bond cleavage: Functional role of Glu113 during bis-Fe(IV) formation in MauG.
Geng et al. (2017)
1 more