› 1j4o

Solution NMR

REFINED NMR STRUCTURE OF THE FHA1 DOMAIN OF YEAST RAD53

Released:
DOI: 10.2210/pdb1j4o/pdb
PDB entry 1j4o coloured by chain, front view.
PDB entry 1j4o coloured by chain, side view.
PDB entry 1j4o coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149539 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
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

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: THE STRUCTURES ARE BASED ON A TOTAL OF 2377 RESTRAINTS. AMONG THEM, 2107 ARE NOE-DERIVED DISTANCE CONSTRAINTS, 192 TALOS-DERIVED DIHEDRAL ANGLE RESTRAINTS, AND 78 RESTRAINTS FROM HYDROGEN BONDS.
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

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