2ipc

X-ray diffraction
2.8Å resolution

Crystal structure of the translocation ATPase SecA from Thermus thermophilus reveals a parallel, head-to-head dimer

Released:

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
Macromolecule:
Protein translocase subunit SecA Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 997 amino acids
Theoretical weight: 114.13 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SIW3 (Residues: 1-997; Coverage: 100%)
Gene names: TTHA1251, secA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL45XU
Spacegroup: P32
Unit cell:
a: 168.623Å b: 168.623Å c: 149.758Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.221 0.221 0.254
Expression system: Escherichia coli