PDBe 4orc

X-ray diffraction
2.7Å resolution

Crystal structure of mammalian calcineurin

Released:
Source organism: Homo sapiens
Entry authors: Ma L, Li SJ, Wang J, Wu JW, Wang ZX

Function and Biology Details

Reaction catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform Chain: A
Molecule details ›
Chain: A
Length: 544 amino acids
Theoretical weight: 61.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW P16298 (Residues: 1-524; Coverage: 100%)
Gene names: CALNA2, CALNB, CNA2, PPP3CB
Sequence domains: Calcineurin-like phosphoesterase
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Calcineurin subunit B type 1 Chain: B
Molecule details ›
Chain: B
Length: 170 amino acids
Theoretical weight: 19.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW P63098 (Residues: 1-170; Coverage: 100%)
Gene names: CNA2, CNB, PPP3R1
Sequence domains:
Structure domains: EF-hand

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P6522
Unit cell:
a: 110.2Å b: 110.2Å c: 282.488Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.218 0.215 0.26
Expression system: Escherichia coli