› 1m63

X-ray diffraction
2.8Å resolution

Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes

Released:
DOI: 10.2210/pdb1m63/pdb
Model geometry
Fit model/data
PDB entry 1m63 coloured by chain, front view.
PDB entry 1m63 coloured by chain, side view.
PDB entry 1m63 coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes.
Huai Q, Kim HY, Liu Y, Zhao Y, Mondragon A, Liu JO, Ke H
Proc Natl Acad Sci U S A 99 12037-42 (2002)
PMID: 12218175

Function and Biology Details

Reactions catalysed: 
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
hetero octamer (preferred)
PDBe Complex ID:
PDB-CPX-158804 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Protein phosphatase 3 catalytic subunit alpha Chains: A, E
Molecule details ›
Chains: A, E
Length: 372 amino acids
Theoretical weight: 42.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q08209 (Residues: 1-372; Coverage: 71%)
Gene names: CALNA, CNA, PPP3CA
Sequence domains: Calcineurin-like phosphoesterase
Structure domains: Purple Acid Phosphatase; chain A, domain 2
Calcineurin subunit B type 1 Chains: B, F
Molecule details ›
Chains: B, F
Length: 169 amino acids
Theoretical weight: 19.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P63098 (Residues: 2-170; Coverage: 99%)
Gene names: CNA2, CNB, PPP3R1
Sequence domains: EF-hand domain pair
Structure domains: EF-hand
Peptidyl-prolyl cis-trans isomerase A Chains: C, G
CYCLOSPORIN A Chains: D, H

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand FE 2 x FE
Ligand CA 8 x CA
6 modified residues:
Ligand DAL 2 x DAL
Ligand MLE 8 x MLE
Ligand MVA 2 x MVA
Ligand BMT 2 x BMT
Ligand ABA 2 x ABA
Ligand SAR 2 x SAR

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P41212
Unit cell:
a: 108.657Å b: 108.657Å c: 316.59Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.26 0.26 0.322
Expression systems:
  • Escherichia coli BL21
  • Not provided

Quick links

Citations

39 review citations

Serine/threonine phosphatases: mechanism through structure.
Shi Y. (2009)
38 more

10 mentions without citation

Structural and functional diversity of EF-hand proteins: Evolutionary perspectives.
Kawasaki et al. (2017)
9 more