› 2y5a

X-ray diffraction
1.25Å resolution

Cytochrome c peroxidase (CCP) W191G bound to 3-aminopyridine

Released:
DOI: 10.2210/pdb2y5a/pdb
PDB entry 2y5a coloured by chain, front view.
PDB entry 2y5a coloured by chain, side view.
PDB entry 2y5a coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Probing the dynamic nature of water molecules and their influences on ligand binding in a model binding site.
Cappel D, Wahlström R, Brenk R, Sotriffer CA
J Chem Inf Model 51 2581-94 (2011)
PMID: 21916516

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: 294 amino acids
Theoretical weight: 33.46 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 3AP 1 x 3AP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 50.853Å b: 75.362Å c: 106.884Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.15 0.164
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Latest developments in molecular docking: 2010-2011 in review.
Yuriev et al. (2013)
2 more