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:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-184608 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Protein phosphatase 2C 16
Molecule details ›
Chains: A, B
Length: 340 amino acids
Theoretical weight: 37.75 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
Sequence domains: Protein phosphatase 2C
Structure domains: PPM-type phosphatase domain
Length: 340 amino acids
Theoretical weight: 37.75 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9CAJ0 (Residues: 172-511; Coverage: 70%)
Sequence domains: Protein phosphatase 2C
Structure domains: PPM-type phosphatase domain
Abscisic acid receptor PYL10
Molecule details ›
Chains: C, D
Length: 183 amino acids
Theoretical weight: 20.66 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
Sequence domains: Polyketide cyclase / dehydrase and lipid transport
Structure domains: Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 4
Length: 183 amino acids
Theoretical weight: 20.66 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
- Canonical: Q8H1R0 (Residues: 1-183; Coverage: 100%)
Sequence domains: Polyketide cyclase / dehydrase and lipid transport
Structure domains: Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 4
