2nsa

X-ray diffraction
1.7Å resolution

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

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
Assembly name:
PDBe Complex ID:
PDB-CPX-194603 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trigger factor Chain: A
Molecule details ›
Chain: A
Length: 170 amino acids
Theoretical weight: 20.45 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WZF8 (Residues: 244-406; Coverage: 38%)
Gene names: TM_0694, tig
Sequence domains: Bacterial trigger factor protein (TF) C-terminus
Structure domains: Trigger factor, C-terminal domain

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4A, RIGAKU RU300
Spacegroup: C2221
Unit cell:
a: 53.84Å b: 74.21Å c: 90.07Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.227 0.227 0.252
Expression system: Escherichia coli