› 3kp8

X-ray diffraction
1.66Å resolution

The thioredoxin-like domain of a VKOR homolog from Synechococcus sp.

Released:
DOI: 10.2210/pdb3kp8/pdb
PDB entry 3kp8 coloured by chain, front view.
PDB entry 3kp8 coloured by chain, side view.
PDB entry 3kp8 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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

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: 106 amino acids
Theoretical weight: 11.57 KDa
Source organism: Synechococcus sp. JA-2-3B'a(2-13)
Expression system: Escherichia coli
UniProt:
  • Canonical: Q2JJF6 (Residues: 186-283; Coverage: 35%)
Gene name: CYB_2278
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P42212
Unit cell:
a: 57.088Å b: 57.088Å c: 57.83Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.194 0.212
Expression system: Escherichia coli

Quick links

Citations

33 review citations

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

3 mentions without citation

Macromolecular ab initio phasing enforcing secondary and tertiary structure.
Millán et al. (2015)
2 more