› 1cig

X-ray diffraction
1.8Å resolution

STRUCTURAL AND FUNCTIONAL EFFECTS OF MULTIPLE MUTATIONS AT DISTAL SITES IN CYTOCHROME C

Released:
DOI: 10.2210/pdb1cig/pdb
PDB entry 1cig coloured by chain, front view.
PDB entry 1cig coloured by chain, side view.
PDB entry 1cig coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structural and functional effects of multiple mutations at distal sites in cytochrome c.
Lo TP, Komar-Panicucci S, Sherman F, McLendon G, Brayer GD
Biochemistry 34 5259-68 (1995)
PMID: 7711047

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 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 HEC 1 x HEC
1 modified residue:
Ligand M3L 1 x M3L

Experiments and Validation Details

Entry percentile scores
Spacegroup: P43212
Unit cell:
a: 36.42Å b: 36.42Å c: 137.03Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 not available not available
Expression system: Not provided

Quick links

Citations

18 citation in other articles

Experimental study of the protein folding landscape: unfolding reactions in cytochrome c.
Milne et al. (1999)
17 more