› 1aej

X-ray diffraction
2.1Å resolution

SPECIFICITY OF LIGAND BINDING TO A BURIED POLAR CAVITY AT THE ACTIVE SITE OF CYTOCHROME C PEROXIDASE (1-VINYLIMIDAZOLE)

Released:
DOI: 10.2210/pdb1aej/pdb
PDB entry 1aej coloured by chain, front view.
PDB entry 1aej coloured by chain, side view.
PDB entry 1aej coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Artificial protein cavities as specific ligand-binding templates: characterization of an engineered heterocyclic cation-binding site that preserves the evolved specificity of the parent protein.
Musah RA, Jensen GM, Bunte SW, Rosenfeld RJ, Goodin DB
J Mol Biol 315 845-57 (2002)
PMID: 11812152

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: Escherichia coli BL21(DE3)
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 NVI 1 x NVI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 108Å b: 77.3Å c: 51.8Å
α: 90° β: 90° γ: 90°
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Predicting Binding Free Energies: Frontiers and Benchmarks.
Mobley et al. (2017)
2 more

3 mentions without citation

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