3luo

X-ray diffraction
2.55Å resolution

Crystal Structure and functional characterization of the thermophilic prolyl isomerase and chaperone SlyD

Released:

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero hexamer
PDBe Complex ID:
PDB-CPX-163762 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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 BL21
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
Suc-Ala-Leu-Pro-Phe-pNA Chain: B
Molecule details ›
Chain: B
Length: 6 amino acids
Theoretical weight: 591 Da
Source organism: Thermus thermophilus HB8
Expression system: Not provided

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: I213
Unit cell:
a: 111.4Å b: 111.4Å c: 111.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.205 0.235
Expression systems:
  • Escherichia coli BL21
  • Not provided