› 5c1v

X-ray diffraction
3.35Å resolution

CRYSTAL STRUCTURE ANALYSIS OF CATALYTIC SUBUNIT OF HUMAN CALCINEURIN

Released:
DOI: 10.2210/pdb5c1v/pdb
PDB entry 5c1v coloured by chain, front view.
PDB entry 5c1v coloured by chain, side view.
PDB entry 5c1v coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Calcineurin Undergoes a Conformational Switch Evoked via Peptidyl-Prolyl Isomerization.
Guasch A, Aranguren-Ibáñez Á, Pérez-Luque R, Aparicio D, Martínez-Høyer S, Mulero MC, Serrano-Candelas E, Pérez-Riba M, Fita I
PLoS One 10 e0134569 (2015)
PMID: 26248042

Function and Biology Details

Reaction catalysed: 
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170606 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein phosphatase 3 catalytic subunit alpha Chains: A, B
Molecule details ›
Chains: A, B
Length: 346 amino acids
Theoretical weight: 39.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q08209 (Residues: 2-346; Coverage: 66%)
Gene names: CALNA, CNA, PPP3CA
Sequence domains: Calcineurin-like phosphoesterase
Structure domains: Purple Acid Phosphatase; chain A, domain 2

Ligands and Environments

3 bound ligands:
Ligand FE 2 x FE
Ligand ZN 2 x ZN
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1, SLS BEAMLINE X06DA
Spacegroup: P6222
Unit cell:
a: 185.008Å b: 185.008Å c: 106.744Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.217 0.216 0.249
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Calcineurin and Its Role in Synaptic Transmission.
Tarasova et al. (2018)
5 other articles

6 mentions without citation

Functional and Regulatory Roles of Fold-Switching Proteins.
Kim et al. (2021)
5 more