1k2n

Solution NMR

Solution Structure of the FHA2 domain of Rad53 Complexed with a Phosphothreonyl Peptide Derived from Rad9

Released:

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase RAD53 Chain: A
Molecule details ›
Chain: A
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%)
Gene names: MEC2, P2588, RAD53, SAD1, SPK1, YPL153C
Sequence domains: FHA domain
Structure domains: Tumour Suppressor Smad4
DNA repair protein RAD9 Chain: P
Molecule details ›
Chain: P
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%)
Gene names: RAD9, YD9934.02C, YDR217C

Ligands and Environments

No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
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