› 4nv5

X-ray diffraction
2.79Å resolution

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

Released:
DOI: 10.2210/pdb4nv5/pdb
PDB entry 4nv5 coloured by chain, front view.
PDB entry 4nv5 coloured by chain, side view.
PDB entry 4nv5 coloured by chain, top view.
Source organism: Synechococcus sp. JA-2-3B'a(2-13)
Primary publication:
Structures of an intramembrane vitamin K epoxide reductase homolog reveal control mechanisms for electron transfer.
Liu S, Cheng W, Fowle Grider R, Shen G, Li W
Nat Commun 5 3110 (2014)
PMID: 24477003

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-173664 (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

Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.
Fass et al. (2018)
5 more

6 mentions without citation

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