› 1f04

Solution NMR

SOLUTION STRUCTURE OF OXIDIZED BOVINE MICROSOMAL CYTOCHROME B5 MUTANT (E44A, E48A, E56A, D60A) AND ITS INTERACTION WITH CYTOCHROME C

Released:
DOI: 10.2210/pdb1f04/pdb
PDB 1f04 coloured by chain and viewed from the front.
PDB 1f04 coloured by chain and viewed from the side.
PDB 1f04 coloured by chain and viewed from the top.
Source organism: Bos taurus
Primary publication:
Solution structure of cytochrome b(5) mutant (E44/48/56A/D60A) and its interaction with cytochrome c.
Wu Y, Wang Y, Qian C, Lu J, Li E, Wang W, Lu J, Xie Y, Wang J, Zhu D, Huang Z, Tang W
Eur. J. Biochem. 268 1620-30 (2001)
PMID: 11248680

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome b5 Chain: A
Molecule details ›
Chain: A
Length: 82 amino acids
Theoretical weight: 9.26 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00171 (Residues: 8-89; Coverage: 61%)
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
Refinement method: TORSION ANGLE MOLECULAR
Expression system: Escherichia coli

Quick links

Citations

6 citation in other articles

Discovery and characterization of a cytochrome b5 variant in humans with impaired hydroxylamine reduction capacity.
Kurian et al. (2007)
5 more

2 mentions without citation

Convergent neofunctionalization by positive Darwinian selection after ancient recurrent duplications of the xanthine dehydrogenase gene.
Rodríguez-Trelles et al. (2003)
1 more