PDBe 1l1p

Solution NMR

Solution Structure of the PPIase Domain from E. coli Trigger Factor

Source organism: Escherichia coli
Entry authors: Kozlov G, Trempe J-F, Perreault A, Wong M, Denisov A, Ghandi S, Gehring K, Ekiel I, Montreal-Kingston Bacterial Structural Genomics Initiative (BSGI)

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

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Trigger factor Chain: A
Molecule details ›
Chain: A
Length: 106 amino acids
Theoretical weight: 11.66 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
  • Canonical: P0A850 (Residues: 148-249; Coverage: 24%)
Gene names: JW0426, b0436, tig
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 62%
Refinement method: simulated annealing
Chemical shifts: BMR5298  
Expression system: Escherichia coli BL21