Function and Biology Details
Reaction catalysed:
ATP + L-seryl/L-threonyl/L-tyrosyl-[protein] = ADP + O-phospho-L-seryl/O-phospho-L-threonyl/O-phospho-L-tyrosyl-[protein]
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-147050 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase RAD53
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 18.15 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: FHA domain
Structure domains: Tumour Suppressor Smad4
Length: 158 amino acids
Theoretical weight: 18.15 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P22216 (Residues: 573-730; Coverage: 19%)
Sequence domains: FHA domain
Structure domains: Tumour Suppressor Smad4
DNA repair protein RAD9
Molecule details ›
Chain: P
Length: 9 amino acids
Theoretical weight: 1.14 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
UniProt:
Length: 9 amino acids
Theoretical weight: 1.14 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
UniProt:
- Canonical: P14737 (Residues: 599-607; Coverage: 1%)
Ligands and Environments
No bound ligands
1 modified residue:
Experiments and Validation Details
Refinement method:
THE COMPLEX STRUCTURES ARE GENERATED USING A TOTAL OF 3369 RESTRAINTS, 3181 DISTANCE RESTRAINTS, AND 188 TALOS-DERIVED DIHEDRAL ANGLE RESTRAINTS.
Expression systems:
- Escherichia coli BL21(DE3)
- Not provided
