› 1dse

X-ray diffraction
2Å resolution

CYTOCHROME C PEROXIDASE H175G MUTANT, IMIDAZOLE COMPLEX, WITH PHOSPHATE BOUND, PH 6, 100K

Released:
DOI: 10.2210/pdb1dse/pdb
PDB entry 1dse coloured by chain, front view.
PDB entry 1dse coloured by chain, side view.
PDB entry 1dse coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Replacement of the axial histidine ligand with imidazole in cytochrome c peroxidase. 1. Effects on structure.
Hirst J, Wilcox SK, Williams PA, Blankenship J, McRee DE, Goodin DB
Biochemistry 40 1265-73 (2001)
PMID: 11170452

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: 292 amino acids
Theoretical weight: 33.24 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
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
2 bound ligands:
Ligand PO4 1 x PO4
Ligand IMD 1 x IMD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P212121
Unit cell:
a: 107.258Å b: 73.768Å c: 51.041Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 not available not available
Expression system: Escherichia coli

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Citations

1 review citation

Heme enzyme structure and function.
Poulos TL. (2014)
11 other articles