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-155965 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Abscisic acid receptor PYL1
Molecule details ›
Chains: A, C
Length: 178 amino acids
Theoretical weight: 20.53 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: 178 amino acids
Theoretical weight: 20.53 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
- Canonical:
Q8VZS8 (Residues: 36-211; Coverage: 80%)
Sequence domains: Polyketide cyclase / dehydrase and lipid transport
Structure domains: Alpha-D-Glucose-1,6-Bisphosphate; Chain A, domain 4
Protein phosphatase 2C 56
Molecule details ›
Chains: B, D
Length: 319 amino acids
Theoretical weight: 35.17 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
Sequence domains: Protein phosphatase 2C
Structure domains: PPM-type phosphatase domain
Length: 319 amino acids
Theoretical weight: 35.17 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
- Canonical: P49597 (Residues: 117-434; Coverage: 73%)
Sequence domains: Protein phosphatase 2C
Structure domains: PPM-type phosphatase domain
