› 5kke

X-ray diffraction
1.7Å resolution

Crystal Structure of a Domain-swapped Dimer of Yeast Iso-1-cytochrome c with CYMAL5

Released:
DOI: 10.2210/pdb5kke/pdb
PDB entry 5kke coloured by chain, front view.
PDB entry 5kke coloured by chain, side view.
PDB entry 5kke coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Cytochrome c Can Form a Well-Defined Binding Pocket for Hydrocarbons.
McClelland LJ, Steele HB, Whitby FG, Mou TC, Holley D, Ross JB, Sprang SR, Bowler BE
J Am Chem Soc 138 16770-16778 (2016)
PMID: 27990813

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132233 (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 S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00044 (Residues: 2-109; Coverage: 99%)
Gene names: CYC1, J1653, YJR048W
Sequence domains: Cytochrome c

Ligands and Environments

5 bound ligands:
Ligand HEC 1 x HEC
Ligand SO4 2 x SO4
Ligand CM5 1 x CM5
Ligand CL 1 x CL
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: I222
Unit cell:
a: 49.74Å b: 69.326Å c: 72.482Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.171 0.204
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

MOMP, cell suicide as a BCL-2 family business.
Kalkavan et al. (2018)
1 more

1 mention without citation

Cytochrome c Can Form a Well-Defined Binding Pocket for Hydrocarbons.
McClelland et al. (2016)