› 2frc

Solution NMR

CYTOCHROME C (REDUCED) FROM EQUUS CABALLUS, NMR, MINIMIZED AVERAGE STRUCTURE

Released:
DOI: 10.2210/pdb2frc/pdb
PDB entry 2frc coloured by chain, front view.
PDB entry 2frc coloured by chain, side view.
PDB entry 2frc coloured by chain, top view.
Source organism: Equus caballus
Primary publication:
Solution structure of horse heart ferricytochrome c and detection of redox-related structural changes by high-resolution 1H NMR.
Qi PX, Beckman RA, Wand AJ
Biochemistry 35 12275-86 (1996)
PMID: 8823161

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132211 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c Chain: A
Molecule details ›
Chain: A
Length: 104 amino acids
Theoretical weight: 11.73 KDa
Source organism: Equus caballus
UniProt:
  • Canonical: P00004 (Residues: 2-105; Coverage: 99%)
Gene names: CYC, CYCS
Sequence domains: Cytochrome c
Structure domains: Cytochrome c-like domain

Ligands and Environments

1 bound ligand:
Ligand HEC 1 x HEC
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: SIMMULATED ANNEALING

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Citations

4 review citations

Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.
Liu et al. (2014)
3 more

3 mentions without citation

Oxidative modification of cytochrome c by singlet oxygen.
Kim et al. (2008)
2 more