Solution NMR

NMR structure of the FHA1 Domain of Rad53 in Complex with a Rad9-derived Phosphothreonine (at T192) Peptide


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:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine/threonine-protein kinase RAD53 Chain: A
Molecule details ›
Chain: A
Length: 151 amino acids
Theoretical weight: 17.09 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P22216 (Residues: 14-164; Coverage: 18%)
Gene names: MEC2, P2588, RAD53, SAD1, SPK1, YPL153C
Sequence domains: FHA domain
Structure domains: Tumour Suppressor Smad4
DNA repair protein RAD9 Chain: B
Molecule details ›
Chain: B
Length: 13 amino acids
Theoretical weight: 1.49 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
  • Canonical: P14737 (Residues: 188-200; 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 structure are generated using a total of 2474 restraints. Among them, 3 artificial constraints, 192 TALOS-derived dihedral angle restraints, 78 H-bond restraints, 22 intermolecular distance constrains, and 2179 intra-FHA1 and intra-peptide distance constraints
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided