Function and Biology Details
Reaction catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Trigger factor
- FKBP-type peptidyl-prolyl cis-trans isomerase domain
- Trigger factor ribosome-binding domain superfamily
- Trigger factor, C-terminal
- Trigger factor/SurA domain superfamily
- Peptidyl-prolyl cis-trans isomerase domain superfamily
- Trigger factor, C-terminal domain superfamily
- Trigger factor, ribosome-binding, bacterial
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Trigger factor (preferred)
PDBe Complex ID:
PDB-CPX-141660 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trigger factor
Molecule details ›
Chains: A, B
Length: 443 amino acids
Theoretical weight: 49.7 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 443 amino acids
Theoretical weight: 49.7 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
- Canonical:
P0A850 (Residues: 1-432; Coverage: 100%)
Sequence domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Chemical shift assignment:
12%
Refinement method:
molecular dynamics
Expression system: Escherichia coli
