Function and Biology Details
Reactions catalysed:
ATP + a protein = ADP + a phosphoprotein
ATP + L-seryl/L-threonyl/L-tyrosyl-[protein] = ADP + O-phospho-L-seryl/O-phospho-L-threonyl/O-phospho-L-tyrosyl-[protein]
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171580 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Mitogen-activated protein kinase 7
Molecule details ›
Chains: A, D
Length: 442 amino acids
Theoretical weight: 49.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Protein kinase domain
Structure domains:
Length: 442 amino acids
Theoretical weight: 49.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q13164 (Residues: 1-431; Coverage: 53%)
Sequence domains: Protein kinase domain
Structure domains:
Dual specificity mitogen-activated protein kinase kinase 5
Molecule details ›
Chains: B, E
Length: 126 amino acids
Theoretical weight: 14.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: PB1 domain
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Length: 126 amino acids
Theoretical weight: 14.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: Q13163 (Residues: 16-130; Coverage: 26%)
Sequence domains: PB1 domain
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
