3jux

X-ray diffraction
3.1Å resolution

Structure of the translocation ATPase SecA from Thermotoga maritima

Released:
Source organism: Thermotoga maritima
Primary publication:
Conformational flexibility and peptide interaction of the translocation ATPase SecA.
J. Mol. Biol. 394 606-12 (2009)
PMID: 19850053

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein translocase subunit SecA Chain: A
Molecule details ›
Chain: A
Length: 822 amino acids
Theoretical weight: 94.92 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X1R4 (Residues: 1-816; Coverage: 94%)
Gene names: TM_1578, secA
Sequence domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 64.533Å b: 119.403Å c: 120.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.227 0.303
Expression system: Escherichia coli