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Solution NMR

A REFINED NMR STRUCTURE OF A NEW PHOPHOPEPTIDE-BINDING DOMAIN CONTAINING THE FHA2 OF RAD53

Released:
DOI: 10.2210/pdb1dmz/pdb
PDB entry 1dmz coloured by chain, ensemble of 20 models, front view.
PDB entry 1dmz coloured by chain, ensemble of 20 models, side view.
PDB entry 1dmz coloured by chain, ensemble of 20 models, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Structure and function of a new phosphopeptide-binding domain containing the FHA2 of Rad53.
Liao H, Byeon IJ, Tsai MD
J Mol Biol 294 1041-9 (1999)
PMID: 10588905

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: 158 amino acids
Theoretical weight: 18.15 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P22216 (Residues: 573-730; Coverage: 19%)
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: simulated annealing
Expression system: Escherichia coli

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Citations

8 review citations

The DNA damage response: putting checkpoints in perspective.
Zhou et al. (2000)
7 more

3 mentions without citation

Advances in Human Immune System Mouse Models for Studying Human Hematopoiesis and Cancer Immunotherapy.
Mian et al. (2020)
2 more