› 1sog

X-ray diffraction
1.85Å resolution

Cyrstal Structure of Cytochrome c Peroxidase Mutant: CcPK2M2

Released:
DOI: 10.2210/pdb1sog/pdb
PDB entry 1sog coloured by chain, front view.
PDB entry 1sog coloured by chain, side view.
PDB entry 1sog coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Electrostatic control of the tryptophan radical in cytochrome c peroxidase.
Barrows TP, Bhaskar B, Poulos TL
Biochemistry 43 8826-34 (2004)
PMID: 15236591

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
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: 33.64 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00431 (Residues: 68-361; 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:
Ligand K 1 x K
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 106.79Å b: 75.86Å c: 51.38Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.166 0.201
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

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

1 mention without citation

Exploring functionally related enzymes using radially distributed properties of active sites around the reacting points of bound ligands.
Ueno et al. (2012)