2b0z

X-ray diffraction
2.7Å resolution

Crystal structure of the protein-protein complex between F82I cytochrome c and cytochrome c peroxidase

Released:
Source organism: Saccharomyces cerevisiae
Primary publication:
Effects of interface mutations on association modes and electron-transfer rates between proteins.
Proc Natl Acad Sci U S A 102 15465-70 (2005)
PMID: 16227441

Function and Biology Details

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-132231 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Cytochrome c peroxidase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 294 amino acids
Theoretical weight: 33.57 KDa
Source organism: Saccharomyces cerevisiae
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: 12.04 KDa
Source organism: Saccharomyces cerevisiae
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 ZNH 1 x ZNH

Cofactor: Ligand HEC 1 x HEC
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 43.802Å b: 51.989Å c: 183.669Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.263 0.262 0.289
Expression system: Escherichia coli