› 1mkr

X-ray diffraction
1.58Å resolution

Crystal Structure of a Mutant Variant of Cytochrome c Peroxidase (Plate like crystals)

Released:
DOI: 10.2210/pdb1mkr/pdb
PDB entry 1mkr coloured by chain, front view.
PDB entry 1mkr coloured by chain, side view.
PDB entry 1mkr coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
A novel heme and peroxide-dependent tryptophan-tyrosine cross-link in a mutant of cytochrome c peroxidase.
Bhaskar B, Immoos CE, Shimizu H, Sulc F, Farmer PJ, Poulos TL
J Mol Biol 328 157-66 (2003)
PMID: 12684005

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: 33.6 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
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 50.48Å b: 50.957Å c: 118.884Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.194 0.219
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

Structure and mechanism in the bacterial dihaem cytochrome c peroxidases.
Pettigrew et al. (2006)
2 more