PDB 1m63 structure summary ‹ Protein Data Bank in Europe (PDBe)

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:

cyclosporin A binding

Biological process:

calcineurin-mediated signaling

Cellular component:

cytosol

Sequence domains:

5 more 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

Molecule details ›

Chains: C, G
Length: 165 amino acids
Theoretical weight: 18.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:

Canonical: P62937 (Residues: 1-165; Coverage: 100%)

Gene names: CYPA, PPIA
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like

CYCLOSPORIN A Chains: D, H

Molecule details ›

Chains: D, H
Length: 11 amino acids
Theoretical weight: 1.22 KDa
Source organism: Tolypocladium inflatum
Expression system: Not provided