2jql

Solution NMR

NMR structure of the yeast Dun1 FHA domain in complex with a doubly phosphorylated (pT) peptide derived from Rad53 SCD1

Released:

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-149543 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
DNA damage response protein kinase DUN1 Chain: A
Molecule details ›
Chain: A
Length: 151 amino acids
Theoretical weight: 17.39 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P39009 (Residues: 19-159; Coverage: 28%)
Gene names: D2370, DUN1, YDL101C
Sequence domains: FHA domain
Structure domains: Tumour Suppressor Smad4
Serine/threonine-protein kinase RAD53 Chain: B
Molecule details ›
Chain: B
Length: 10 amino acids
Theoretical weight: 1.28 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
UniProt:
  • Canonical: P22216 (Residues: 3-12; Coverage: 1%)
Gene names: MEC2, P2588, RAD53, SAD1, SPK1, YPL153C

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided