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REFINED NMR STRUCTURE OF THE FHA1 DOMAIN OF YEAST RAD53
Summary
Header TRANSFERASEsearch
Method SOLUTION NMR
Experiment Spacegroup: P 1
Released 05/12/2001, deposition: 03/10/2001, last revision: 24/02/2009
Authors Yuan, C.search; Yongkiettrakul, S.search; Byeon, I.-J.L.search; Zhou, S.search; Tsai, M.-D.search
Primary citation Solution structures of two FHA1-phosphothreonine peptide complexes provide insight into the structural basis of the ligand specificity of FHA1 from yeast Rad53.
J.MOL.BIOL.search vol:314, pag:563-575 (2001) [PubMed ID 11846567 ]search
Keywords FHA DOMAINsearch, RAD53search, RAD9search, PHOSPHOTHREONINEsearch, PHOSPHOPROTEINsearch, NMRsearch, TRANSFERASEsearch
EC 2.7.11.1 ExPASy BRENDA search (A)
Organism Saccharomyces cerevisiae(baker's yeast) 4932search(A)
UniProt Serine/threonine-protein kinase RAD53 (EC 2.7.11.1) (Serine-protein kinase 1) (CHK2 homolog) P22216search (A)
Polymers
Id Name Type UniProt Residues Observed
A PROTEIN KINASE SPK1 Protein P22216 (RAD53_YEAST)search
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