Function and Biology Details
Reaction catalysed:
[(1) L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)., (2) L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP +H(+)., (1) L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)., (2) L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP +H(+)., (1) L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H(+)., (2) L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP +H(+).]
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domain:
Structure analysis Details
Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-195262 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Receptor-interacting serine/threonine-protein kinase 3
Molecule details ›
Chains: A, B, C
Length: 141 amino acids
Theoretical weight: 15.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: RIP homotypic interaction motif
Length: 141 amino acids
Theoretical weight: 15.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9Y572 (Residues: 388-518; Coverage: 25%)
Sequence domains: RIP homotypic interaction motif
