PDBe 2nsb

X-ray diffraction
3.2Å resolution

Structures of and interactions between domains of trigger factor from Themotoga maritima

Released:
Source organism: Thermotoga maritima
Primary publication:
Structures of and interactions between domains of trigger factor from Thermotoga maritima.
Acta Crystallogr. D Biol. Crystallogr. 63 536-47 (2007)
PMID: 17372359

Function and Biology Details

Reaction catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0). 
Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trigger factor Chain: A
Molecule details ›
Chain: A
Length: 109 amino acids
Theoretical weight: 12.82 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WZF8 (Residues: 1-109; Coverage: 26%)
Gene names: TM_0694, tig

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P21212
Unit cell:
a: 48.092Å b: 86.553Å c: 32.954Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.262 0.256 0.262
Expression system: Escherichia coli