4cvi

Hybrid

Neutron Structure of Ferric Cytochrome c Peroxidase - Deuterium exchanged at room temperature

Released:

Function and Biology Details

Reaction catalysed:
2 ferrocytochrome c + H(2)O(2) = 2 ferricytochrome c + 2 H(2)O
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-132475 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c peroxidase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 294 amino acids
Theoretical weight: 33.63 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00431 (Residues: 70-361; Coverage: 81%)
Gene names: CCP, CCP1, CPO, YKR066C
Sequence domains: Peroxidase
Structure domains:

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM
1 bound ligand:
No modified residues

Experiments and Validation Details

Experimental Method: Neutron Diffraction, X-ray diffraction
X-ray source: Xenocs GeniX 3D Cu HF, ILL BEAMLINE LADI III
Spacegroup: P212121
Unit cell:
a: 51.7Å b: 76.8Å c: 107.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.138 0.134 0.177
Expression system: Escherichia coli BL21(DE3)