› 1cmp

X-ray diffraction
1.9Å resolution

SMALL MOLECULE BINDING TO AN ARTIFICIALLY CREATED CAVITY AT THE ACTIVE SITE OF CYTOCHROME C PEROXIDASE

Released:
DOI: 10.2210/pdb1cmp/pdb
PDB entry 1cmp coloured by chain, front view.
PDB entry 1cmp coloured by chain, side view.
PDB entry 1cmp coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Small molecule binding to an artificially created cavity at the active site of cytochrome c peroxidase.
Fitzgerald MM, Churchill MJ, McRee DE, Goodin DB
Biochemistry 33 3807-18 (1994)
PMID: 8142383

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: 33.46 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Not provided
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 DMI 1 x DMI
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 105.2Å b: 74.3Å c: 45.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 not available
Expression system: Not provided

Quick links

Citations

6 review citations

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

1 mention without citation

Probing molecular docking in a charged model binding site.
Brenk et al. (2006)