› 1hko

Solution NMR

NMR structure of bovine cytochrome b5

Released:
DOI: 10.2210/pdb1hko/pdb
PDB entry 1hko coloured by chain, ensemble of 42 models, front view.
PDB entry 1hko coloured by chain, ensemble of 42 models, side view.
PDB entry 1hko coloured by chain, ensemble of 42 models, top view.
Source organism: Bos taurus
Primary publication:
The solution structure of bovine ferricytochrome b5 determined using heteronuclear NMR methods.
Muskett FW, Kelly GP, Whitford D
J Mol Biol 258 172-89 (1996)
PMID: 8613986

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132303 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome b5 Chain: A
Molecule details ›
Chain: A
Length: 104 amino acids
Theoretical weight: 11.81 KDa
Source organism: Bos taurus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P00171 (Residues: 2-105; Coverage: 78%)
Gene names: CYB5, CYB5A
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 1 x HEM
No modified residues

Experiments and Validation Details

Entry percentile scores
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

The molecular biology, biochemistry, and physiology of human steroidogenesis and its disorders.
Miller et al. (2011)
2 more

4 mentions without citation

Evolutionary remodeling of βγ-crystallins for domain stability at cost of Ca2+ binding.
Suman et al. (2011)
3 more