› 3cgn

X-ray diffraction
2.7Å resolution

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-178159 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase Chain: A
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 17.4 KDa
Source organism: Thermus thermophilus HB8
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5SLE7 (Residues: 1-149; Coverage: 100%)
Gene name: TTHA0346
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.2
Spacegroup: F222
Unit cell:
a: 81.18Å b: 85.09Å c: 92.22Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.209 0.257
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Prolyl isomerization and its catalysis in protein folding and protein function.
Schmidpeter et al. (2015)
1 more

3 mentions without citation

Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD.
Quistgaard et al. (2016)
2 more