› 1j4p

Solution NMR

NMR STRUCTURE OF THE FHA1 DOMAIN OF RAD53 IN COMPLEX WITH A RAD9-DERIVED PHOSPHOTHREONINE (AT T155) PEPTIDE

Released:
DOI: 10.2210/pdb1j4p/pdb
PDB entry 1j4p coloured by chain, front view.
PDB entry 1j4p coloured by chain, side view.
PDB entry 1j4p coloured by chain, 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: 1.62 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Not provided
UniProt:
  • Canonical: P14737 (Residues: 149-161; 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 STRUCTURES ARE GENERATED USING A TOTAL OF 2438 RESTRAINTS. AMONG THEM, 3 ARTIFICAL CONSTRAINTS, 192 TALOS- DERIVED DIHEDRAL ANGLE RESTRAINS, 78 RESTRAINTS FROM H-BOND, 16 INTERMOLECULAR DISTANCE CONSTRAINS, AND 2149 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

1 mention without citation

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