› 2ruq

Solution NMR

solution structure of human Pin1 PPIase mutant C113A

Released:
DOI: 10.2210/pdb2ruq/pdb
PDB entry 2ruq coloured by chain, ensemble of 10 models, front view.
PDB entry 2ruq coloured by chain, ensemble of 10 models, side view.
PDB entry 2ruq coloured by chain, ensemble of 10 models, top view.
Source organism: Homo sapiens
Primary publication:
Allosteric Breakage of the Hydrogen Bond within the Dual-Histidine Motif in the Active Site of Human Pin1 PPIase.
Wang J, Tochio N, Kawasaki R, Tamari Y, Xu N, Uewaki J, Utsunomiya-Tate N, Tate S
Biochemistry 54 5242-53 (2015)
PMID: 26226559

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence 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: 117 amino acids
Theoretical weight: 13.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q13526 (Residues: 51-163; Coverage: 69%)
Gene name: PIN1
Sequence domains: PPIC-type PPIASE domain
Structure domains: Chitinase A; domain 3

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 92%
Refinement method: distance geometry
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

Disordered linkers in multidomain allosteric proteins: Entropic effect to favor the open state or enhanced local concentration to favor the closed state?
Li et al. (2018)
7 more