› 1awp

X-ray diffraction
2Å resolution

RAT OUTER MITOCHONDRIAL MEMBRANE CYTOCHROME B5

Released:
DOI: 10.2210/pdb1awp/pdb
PDB entry 1awp coloured by chain, front view.
PDB entry 1awp coloured by chain, side view.
PDB entry 1awp coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
The reduction potential of cytochrome b5 is modulated by its exposed heme edge.
Rivera M, Seetharaman R, Girdhar D, Wirtz M, Zhang X, Wang X, White S
Biochemistry 37 1485-94 (1998)
PMID: 9484218

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137475 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome b5 type B Chains: A, B
Molecule details ›
Chains: A, B
Length: 92 amino acids
Theoretical weight: 10.42 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P04166 (Residues: 12-103; Coverage: 63%)
Gene names: Cyb5b, Cyb5m, Omb5
Sequence domains: Cytochrome b5-like Heme/Steroid binding domain
Structure domains: Cytochrome b5-like heme/steroid binding domain

Ligands and Environments

1 bound ligand:
Ligand HEM 2 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 45.64Å b: 71.19Å c: 73.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 0.225
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

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

1 mention without citation

Unique structure of Ascaris suum b5-type cytochrome: an additional alpha-helix and positively charged residues on the surface domain interact with redox partners.
Yokota et al. (2006)