X-ray diffraction
3Å resolution

Crystal structure of Mg-ADP-bound SecA from Bacillus subtilis


Function and Biology Details

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Protein translocase subunit SecA Chain: A
Molecule details ›
Chain: A
Length: 802 amino acids
Theoretical weight: 91.39 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P28366 (Residues: 1-802; Coverage: 95%)
Gene names: BSU35300, div+, secA
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID2
Spacegroup: P3112
Unit cell:
a: 131.245Å b: 131.245Å c: 150.453Å
α: 90° β: 90° γ: 120°
R R work R free
0.217 0.217 0.291
Expression system: Escherichia coli BL21(DE3)