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:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189947 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Abscisic acid receptor PYL3
Molecule details ›
Chain: A
Length: 182 amino acids
Theoretical weight: 20.6 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: 182 amino acids
Theoretical weight: 20.6 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9SSM7 (Residues: 24-205; Coverage: 87%)
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: 335 amino acids
Theoretical weight: 37.13 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
Sequence domains: Protein phosphatase 2C
Structure domains: PPM-type phosphatase domain
Length: 335 amino acids
Theoretical weight: 37.13 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
- Canonical: Q9CAJ0 (Residues: 172-506; Coverage: 69%)
Sequence domains: Protein phosphatase 2C
Structure domains: PPM-type phosphatase domain
