› 1k3q

Solution NMR

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

Released:
DOI: 10.2210/pdb1k3q/pdb
PDB entry 1k3q coloured by chain, ensemble of 20 models, front view.
PDB entry 1k3q coloured by chain, ensemble of 20 models, side view.
PDB entry 1k3q coloured by chain, ensemble of 20 models, top view.
Source organisms:
Primary publication:
Solution structures of two FHA1-phosphothreonine peptide complexes provide insight into the structural basis of the ligand specificity of FHA1 from yeast Rad53.
Yuan C, Yongkiettrakul S, Byeon IJ, Zhou S, Tsai MD
J Mol Biol 314 563-75 (2001)
PMID: 11846567

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 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)
UniProt:
  • 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
UniProt:
  • Canonical: P14737 (Residues: 188-200; Coverage: 1%)
Gene names: RAD9, YD9934.02C, YDR217C

Ligands and Environments

No bound ligands
1 modified residue:
Ligand TPO 1 x TPO

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

Quick links

Citations

3 review citations

The Chk2 protein kinase.
Ahn et al. (2004)
2 more

3 mentions without citation

Damped-dynamics flexible fitting.
Kovacs et al. (2008)
2 more