› 1nmv

Solution NMR

Solution structure of human Pin1

Released:
DOI: 10.2210/pdb1nmv/pdb
PDB entry 1nmv coloured by chain, ensemble of 10 models, front view.
PDB entry 1nmv coloured by chain, ensemble of 10 models, side view.
PDB entry 1nmv coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Structural analysis of the mitotic regulator hPin1 in solution: insights into domain architecture and substrate binding.
Bayer E, Goettsch S, Mueller JW, Griewel B, Guiberman E, Mayr LM, Bayer P
J Biol Chem 278 26183-93 (2003)
PMID: 12721297

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171737 (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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Pinning down cell signaling, cancer and Alzheimer's disease.
Lu KP. (2004)
8 more

20 mentions without citation

Roles of Prolyl Isomerases in RNA-Mediated Gene Expression.
Thapar R. (2015)
19 more