› 2icv

X-ray diffraction
1.6Å resolution

Kinetic and Crystallographic Studies of a Redesigned Manganese-Binding Site in Cytochrome c Peroxidase

Released:
DOI: 10.2210/pdb2icv/pdb
PDB entry 2icv coloured by chain, front view.
PDB entry 2icv coloured by chain, side view.
PDB entry 2icv coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Kinetic and crystallographic studies of a redesigned manganese-binding site in cytochrome c peroxidase.
Pfister TD, Mirarefi AY, Gengenbach AJ, Zhao X, Danstrom C, Conatser N, Gao YG, Robinson H, Zukoski CF, Wang AH, Lu Y
J Biol Inorg Chem 12 126-37 (2007)
PMID: 17021923

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 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: 291 amino acids
Theoretical weight: 33.26 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P00431 (Residues: 71-361; 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 CO 1 x CO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12C
Spacegroup: P212121
Unit cell:
a: 43.958Å b: 52.477Å c: 136.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.223 0.257
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Substrate oxidation sites in versatile peroxidase and other basidiomycete peroxidases.
Ruiz-Dueñas et al. (2009)
4 more

1 mention without citation

Enhancing Mn(II)-Binding and Manganese Peroxidase Activity in a Designed Cytochrome c Peroxidase through Fine-Tuning Secondary-Sphere Interactions.
Hosseinzadeh et al. (2016)