› 3kp9

X-ray diffraction
3.6Å resolution

Structure of a bacterial homolog of vitamin K epoxide reductase

Released:
DOI: 10.2210/pdb3kp9/pdb
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PDB entry 3kp9 coloured by chain, front view.
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PDB entry 3kp9 coloured by chain, top view.
Source organism: Synechococcus sp. JA-2-3B'a(2-13)
Primary publication:
Structure of a bacterial homologue of vitamin K epoxide reductase.
Li W, Schulman S, Dutton RJ, Boyd D, Beckwith J, Rapoport TA
OpenAccess logo Nature 463 507-12 (2010)
PMID: 20110994

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 Chain: A
Molecule details ›
Chain: A
Length: 291 amino acids
Theoretical weight: 31.67 KDa
Source organism: Synechococcus sp. JA-2-3B'a(2-13)
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2JJF6 (Residues: 1-283; Coverage: 100%)
Gene name: CYB_2278
Sequence domains: Vitamin K epoxide reductase family
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand U10 1 x U10
Ligand HG 2 x HG
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P61
Unit cell:
a: 136.942Å b: 136.942Å c: 68.48Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.256 0.251 0.305
Expression system: Escherichia coli

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Citations

30 review citations

Glutathione peroxidases.
Brigelius-Flohé et al. (2013)
29 more

24 mentions without citation

Disulfide bond formation in the bacterial periplasm: major achievements and challenges ahead.
Denoncin et al. (2013)
23 more

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