› 1irw

X-ray diffraction
2Å resolution

CYTOCHROME C ISOZYME 1, REDUCED, MUTANT WITH ASN 52 REPLACED BY ALA AND CYS 102 REPLACED BY THR

Released:
DOI: 10.2210/pdb1irw/pdb
PDB entry 1irw coloured by chain, front view.
PDB entry 1irw coloured by chain, side view.
PDB entry 1irw coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Mechanistic and structural contributions of critical surface and internal residues to cytochrome c electron transfer reactivity.
Rafferty SP, Guillemette JG, Berghuis AM, Smith M, Brayer GD, Mauk AG
Biochemistry 35 10784-92 (1996)
PMID: 8718869

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-132226 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome c isoform 1 Chain: A
Molecule details ›
Chain: A
Length: 108 amino acids
Theoretical weight: 12.07 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Not provided
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

2 bound ligands:
Ligand SO4 1 x SO4
Ligand HEM 1 x HEM
1 modified residue:
Ligand M3L 1 x M3L

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 36.52Å b: 36.52Å c: 137.39Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.183 0.183 not available
Expression system: Not provided

Quick links

Citations

2 review citations

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