› 2n18

Solution NMR

Dominant form of the low-affinity complex of yeast cytochrome c and cytochrome c peroxidase

Released:
DOI: 10.2210/pdb2n18/pdb
PDB entry 2n18 coloured by chain, ensemble of 15 models, front view.
PDB entry 2n18 coloured by chain, ensemble of 15 models, side view.
PDB entry 2n18 coloured by chain, ensemble of 15 models, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
The low-affinity complex of cytochrome c and its peroxidase.
Van de Water K, Sterckx YG, Volkov AN
Nat Commun 6 7073 (2015)
PMID: 25944250

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:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132227 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Cytochrome c peroxidase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 294 amino acids
Theoretical weight: 33.54 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P00431 (Residues: 68-361; Coverage: 81%)
Gene names: CCP, CCP1, CPO, YKR066C
Sequence domains: Peroxidase
Structure domains:
Cytochrome c isoform 1 Chain: B
Molecule details ›
Chain: B
Length: 108 amino acids
Theoretical weight: 12.07 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P00044 (Residues: 3-109; Coverage: 98%)
Gene names: CYC1, J1653, YJR048W
Sequence domains: Cytochrome c
Structure domains: Cytochrome c-like domain
Cytochrome c isoform 1 Chain: C
Molecule details ›
Chain: C
Length: 108 amino acids
Theoretical weight: 12.07 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: P00044 (Residues: 2-109; Coverage: 99%)
Gene names: CYC1, J1653, YJR048W
Sequence domains: Cytochrome c
Structure domains: Cytochrome c-like domain

Ligands and Environments


Cofactor: Ligand HEM 1 x HEM

Cofactor: Ligand HEC 2 x HEC
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 7%
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

Tuning Radical Relay Residues by Proton Management Rescues Protein Electron Hopping.
Yee et al. (2019)
5 more

1 mention without citation

The low-affinity complex of cytochrome c and its peroxidase.
Van de Water et al. (2015)