5c1v

X-ray diffraction
3.35Å resolution

CRYSTAL STRUCTURE ANALYSIS OF CATALYTIC SUBUNIT OF HUMAN CALCINEURIN

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine/threonine-protein phosphatase 2B catalytic subunit alpha isoform 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%)
  • Best match: Q08209-4 (Residues: 2-86)
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:

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