1tm6

Solution NMR

NMR Structure of the Free Zinc Binding C-terminal Domain of SecA

Released:
Source organism: Escherichia coli
Primary publication:
NMR structure of the C-terminal domain of SecA in the free state.
Biochim Biophys Acta 1702 163-71 (2004)
PMID: 15488768

Function and Biology Details

Reaction catalysed:
ATP + H(2)O + cellular protein(Side 1) = ADP + phosphate + cellular protein(Side 2)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-145293 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein translocase subunit SecA Chain: A
Molecule details ›
Chain: A
Length: 22 amino acids
Theoretical weight: 2.44 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P10408 (Residues: 880-901; Coverage: 2%)
Gene names: JW0096, azi, b0098, pea, prlD, secA
Sequence domains: SEC-C motif

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: standard x-plor protocol; 1. distance geometry sub-embed 2. distance geometry full embed 3. simulated annealing 4. simulated annealing refine