Function and Biology Details
Reactions catalysed:
ATP + L-seryl/L-threonyl/L-tyrosyl-[protein] = ADP + O-phospho-L-seryl/O-phospho-L-threonyl/O-phospho-L-tyrosyl-[protein]
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147202 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Dual specificity mitogen-activated protein kinase kinase 1
Molecule details ›
Chains: A, D, E, H
Length: 341 amino acids
Theoretical weight: 37.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Protein kinase domain
Structure domains:
Length: 341 amino acids
Theoretical weight: 37.93 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q02750 (Residues: 62-393; Coverage: 85%)
Sequence domains: Protein kinase domain
Structure domains:
Serine/threonine-protein kinase B-raf
Molecule details ›
Chains: B, C, F, G
Length: 308 amino acids
Theoretical weight: 35.35 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:
Length: 308 amino acids
Theoretical weight: 35.35 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
- Canonical: P15056 (Residues: 432-726; Coverage: 39%)
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains:
