4tns

X-ray diffraction
1.33Å resolution

Structure of Pin1 PPIase domain bound with all-trans retinoic acid

Released:
Source organism: Homo sapiens
Entry authors: Li WZ, Zhang Y

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-171737 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 151 amino acids
Theoretical weight: 16.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13526 (Residues: 43-163; Coverage: 74%)
Gene name: PIN1
Sequence domains: PPIC-type PPIASE domain
Structure domains: Chitinase A; domain 3

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: C2
Unit cell:
a: 117.806Å b: 36.294Å c: 51.703Å
α: 90° β: 100.92° γ: 90°
R-values:
R R work R free
0.17 0.169 0.187
Expression system: Escherichia coli