› 6mv1

X-ray diffraction
2.15Å resolution

2.15A resolution structure of the CS-b5R domains of human Ncb5or (NAD+ form)

Released:
DOI: 10.2210/pdb6mv1/pdb
PDB entry 6mv1 coloured by chain, front view.
PDB entry 6mv1 coloured by chain, side view.
PDB entry 6mv1 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of the naturally fused CS and cytochrome b5 reductase (b5R) domains of Ncb5or reveal an expanded CS fold, extensive CS-b5R interactions and productive binding of the NAD(P)+ nicotinamide ring.
Benson DR, Lovell S, Mehzabeen N, Galeva N, Cooper A, Gao P, Battaile KP, Zhu H
Acta Crystallogr D Struct Biol 75 628-638 (2019)
PMID: 31282472

Function and Biology Details

Reaction catalysed: 
NADH + 2 ferricytochrome b5 = NAD(+) + H(+) + 2 ferrocytochrome b5
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181621 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cytochrome b5 reductase 4 Chain: A
Molecule details ›
Chain: A
Length: 367 amino acids
Theoretical weight: 42.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7L1T6 (Residues: 164-521; Coverage: 69%)
Gene names: CYB5R4, NCB5OR
Sequence domains:

Ligands and Environments


Cofactor: Ligand FAD 1 x FAD

Cofactor: Ligand NAD 1 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P21
Unit cell:
a: 56.137Å b: 68.628Å c: 57.598Å
α: 90° β: 97.51° γ: 90°
R-values:
R R work R free
0.185 0.183 0.23
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Human Hsp90 cochaperones: perspectives on tissue-specific expression and identification of cochaperones with similar in vivo functions.
Dean et al. (2021)
2 more

1 mention without citation

Crystal structures of the naturally fused CS and cytochrome b5 reductase (b5R) domains of Ncb5or reveal an expanded CS fold, extensive CS-b5R interactions and productive binding of the NAD(P)+ nicotinamide ring.
Benson et al. (2019)