› 4nv5

X-ray diffraction
2.79Å resolution

C50A mutant of Synechococcus VKOR, C2 crystal form (dehydrated)

Released:
DOI: 10.2210/pdb4nv5/pdb
PDB 4nv5 coloured by chain and viewed from the front.
PDB 4nv5 coloured by chain and viewed from the side.
PDB 4nv5 coloured by chain and viewed from the top.
Source organism: Synechococcus sp. JA-2-3B'a(2-13)
Entry authors: Liu S, Cheng W, Fowle Grider R, Shen G, Li W

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Vitamin K epoxide reductase homolog Chains: A, B
Molecule details ›
Chains: A, B
Length: 291 amino acids
Theoretical weight: 31.65 KDa
Source organism: Synechococcus sp. JA-2-3B'a(2-13)
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q2JJF6 (Residues: 1-283; Coverage: 100%)
Gene name: CYB_2278
Sequence domains: Vitamin K epoxide reductase family
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand U10 2 x U10
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: C2
Unit cell:
a: 140.842Å b: 118.822Å c: 68.034Å
α: 90° β: 89.85° γ: 90°
R-values:
R R work R free
0.234 0.232 0.245
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

Oxidative protein folding: state-of-the-art and current avenues of research in plants.
Meyer et al. (2019)
5 more

3 mentions without citation

Structures of an intramembrane vitamin K epoxide reductase homolog reveal control mechanisms for electron transfer.
Liu et al. (2014)
2 more