X-ray diffraction
2.18Å resolution

Crystal structure of SecA in an open conformation from Bacillus Subtilis

Source organism: Bacillus subtilis
Primary publication:
A large conformational change of the translocation ATPase SecA.
Proc. Natl. Acad. Sci. U.S.A. 101 10937-42 (2004)
PMID: 15256599

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Protein translocase subunit SecA Chain: A
Molecule details ›
Chain: A
Length: 844 amino acids
Theoretical weight: 95.96 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli
  • Canonical: P28366 (Residues: 1-841; Coverage: 100%)
Gene names: BSU35300, div+, secA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 149.232Å b: 107.189Å c: 72.054Å
α: 90° β: 94.96° γ: 90°
R R work R free
0.241 0.241 0.273
Expression system: Escherichia coli