› 1pin

X-ray diffraction
1.35Å resolution

PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS

Released:
DOI: 10.2210/pdb1pin/pdb
PDB entry 1pin coloured by chain, front view.
PDB entry 1pin coloured by chain, side view.
PDB entry 1pin coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent.
Ranganathan R, Lu KP, Hunter T, Noel JP
Cell 89 875-86 (1997)
PMID: 9200606

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171740 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 Chain: A
Molecule details ›
Chain: A
Length: 163 amino acids
Theoretical weight: 18.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q13526 (Residues: 1-163; Coverage: 100%)
Gene name: PIN1
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand ALA 1 x ALA
Ligand PRO 1 x PRO
Ligand SO4 1 x SO4
Ligand 1PG 2 x 1PG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P43212
Unit cell:
a: 49Å b: 49Å c: 137.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.223 0.266
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

68 review citations

The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains.
Kay et al. (2000)
67 more

98 mentions without citation

Roles of beta-turns in protein folding: from peptide models to protein engineering.
Marcelino et al. (2008)
97 more