› 1j2m

Solution NMR

Solution structure of CPI-17(22-120)

Released:
DOI: 10.2210/pdb1j2m/pdb
PDB entry 1j2m coloured by chain, front view.
PDB entry 1j2m coloured by chain, side view.
PDB entry 1j2m coloured by chain, top view.
Source organism: Sus scrofa
Primary publication:
Distinctive solution conformation of phosphatase inhibitor CPI-17 substituted with aspartate at the phosphorylation-site threonine residue.
Ohki Sy, Eto M, Shimizu M, Takada R, Brautigan DL, Kainosho M
J Mol Biol 326 1539-47 (2003)
PMID: 12595264

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127584 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein phosphatase 1 regulatory subunit 14A Chain: A
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 11.55 KDa
Source organism: Sus scrofa
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O18734 (Residues: 22-120; Coverage: 67%)
Gene name: CPI17
Sequence domains: PKC-activated protein phosphatase-1 inhibitor
Structure domains: CPI-17

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry simulated annealing
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

Diversity and plasticity in signaling pathways that regulate smooth muscle responsiveness: Paradigms and paradoxes for the myosin phosphatase, the master regulator of smooth muscle contraction.
Eto et al. (2017)
1 more