› 1csu

X-ray diffraction
1.81Å resolution

REPLACEMENTS IN A CONSERVED LEUCINE CLUSTER IN THE HYDROPHOBIC HEME POCKET OF CYTOCHROME C

Released:
DOI: 10.2210/pdb1csu/pdb
PDB entry 1csu coloured by chain, front view.
PDB entry 1csu coloured by chain, side view.
PDB entry 1csu coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Replacements in a conserved leucine cluster in the hydrophobic heme pocket of cytochrome c.
Lo TP, Murphy ME, Guillemette JG, Smith M, Brayer GD
Protein Sci 4 198-208 (1995)
PMID: 7757009

Function and Biology Details

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

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: 12.1 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: 36.51Å b: 36.51Å c: 137.11Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 not available not available
Expression system: Not provided

Quick links

Citations

7 citation in other articles

Many faces of the unfolded state: conformational heterogeneity in denatured yeast cytochrome C.
Pletneva et al. (2005)
6 more

1 mention without citation

Dihydroorotase from the hyperthermophile Aquifex aeolicus is activated by stoichiometric association with aspartate transcarbamoylase and forms a one-pot reactor for pyrimidine biosynthesis.
Zhang et al. (2009)