› 5uy9

X-ray diffraction
1.85Å resolution

Prolyl isomerase Pin1 R14A mutant bound with Brd4 peptide

Released:
DOI: 10.2210/pdb5uy9/pdb
PDB entry 5uy9 coloured by chain, front view.
PDB entry 5uy9 coloured by chain, side view.
PDB entry 5uy9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Prolyl isomerase PIN1 regulates the stability, transcriptional activity and oncogenic potential of BRD4.
Hu X, Dong SH, Chen J, Zhou XZ, Chen R, Nair S, Lu KP, Chen LF
Oncogene 36 5177-5188 (2017)
PMID: 28481868

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-166186 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 Chain: A
Molecule details ›
Chain: A
Length: 163 amino acids
Theoretical weight: 18.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13526 (Residues: 1-163; Coverage: 100%)
Gene name: PIN1
Sequence domains:
Structure domains:
Brd4 peptide Chain: B
Molecule details ›
Chain: B
Length: 7 amino acids
Theoretical weight: 860 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand PE4 1 x PE4
Ligand SO4 2 x SO4
1 modified residue:
Ligand TPO 1 x TPO

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P3121
Unit cell:
a: 68.534Å b: 68.534Å c: 79.64Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.235 0.232 0.291
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

11 review citations

Function of PIN1 in Cancer Development and Its Inhibitors as Cancer Therapeutics.
Yu et al. (2020)
10 more

1 mention without citation

Regulation of eukaryotic protein kinases by Pin1, a peptidyl-prolyl isomerase.
Chen et al. (2023)