X-ray diffraction
3Å resolution

Crystal structure of the isolated DEAD motor domains from Escherichia coli SecA


Function and Biology Details

Reaction catalysed:
ATP + H(2)O + cellular protein(Side 1) = ADP + phosphate + cellular protein(Side 2)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Protein translocase subunit SecA Chains: A, B
Molecule details ›
Chains: A, B
Length: 471 amino acids
Theoretical weight: 52.61 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
  • Canonical: P10408 (Residues: 6-609; Coverage: 52%)
Gene names: JW0096, azi, b0098, pea, prlD, secA
Sequence domains: SecA DEAD-like domain
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 177.823Å b: 71.361Å c: 119.536Å
α: 90° β: 128.82° γ: 90°
R R work R free
0.245 0.245 0.305
Expression system: Escherichia coli