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-100358 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Abscisic acid receptor PYL1
Molecule details ›
Chain: A
Length: 209 amino acids
Theoretical weight: 23.29 KDa
Source organism: Citrus sinensis
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: 209 amino acids
Theoretical weight: 23.29 KDa
Source organism: Citrus sinensis
Expression system: Escherichia coli
UniProt:
- Canonical:
A0A067E666 (Residues: 1-209; Coverage: 100%)
Sequence domains: Polyketide cyclase / dehydrase and lipid transport
Structure domains: Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 4
Protein phosphatase 2C 16
Molecule details ›
Chain: B
Length: 333 amino acids
Theoretical weight: 37.03 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
Sequence domains: Protein phosphatase 2C
Structure domains: PPM-type phosphatase domain
Length: 333 amino acids
Theoretical weight: 37.03 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
- Canonical: Q9CAJ0 (Residues: 179-511; Coverage: 68%)
Sequence domains: Protein phosphatase 2C
Structure domains: PPM-type phosphatase domain
