› 5gv8

X-ray diffraction
0.78Å resolution

Structure of NADH-cytochrome b5 reductase refined with the multipolar atomic model at 0.78A

Released:
DOI: 10.2210/pdb5gv8/pdb
PDB entry 5gv8 coloured by chain, front view.
PDB entry 5gv8 coloured by chain, side view.
PDB entry 5gv8 coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Distribution of valence electrons of the flavin cofactor in NADH-cytochrome b5 reductase.
Takaba K, Takeda K, Kosugi M, Tamada T, Miki K
Sci Rep 7 43162 (2017)
PMID: 28225078

Function and Biology Details

Reaction catalysed: 
NADH + 2 ferricytochrome b5 = NAD(+) + H(+) + 2 ferrocytochrome b5
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160717 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NADH-cytochrome b5 reductase 3 Chain: A
Molecule details ›
Chain: A
Length: 272 amino acids
Theoretical weight: 30.87 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli
UniProt:
  • Canonical: P83686 (Residues: 1-272; Coverage: 100%)
Gene names: CYB5R3, DIA1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD
1 bound ligand:
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 48.48Å b: 72.108Å c: 84.908Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.122 0.122 0.14
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Structural Features of Cytochrome b5-Cytochrome b5 Reductase Complex Formation and Implications for the Intramolecular Dynamics of Cytochrome b5 Reductase.
Gutiérrez-Merino et al. (2021)
1 more

1 mention without citation

Distribution of valence electrons of the flavin cofactor in NADH-cytochrome b5 reductase.
Takaba et al. (2017)