2a0t

NMR structure of the FHA1 domain of Rad53 in complex with a biological relevant phosphopeptide derived from Madt1NMR structure of the FHA1 domain of Rad53 in complex with a biological relevant phosphopeptide derived from Madt1

Structural highlights 2a0t is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: Gene: SPK1 or Rad53 (Saccharomyces cerevisiae) Activity: Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Combinatorial library screens based on binding affinity may preferentially select ligands with ability for ionic interactions and miss the biologically relevant ligands that bind more weakly with predominantly hydrophobic interactions. FHA domain-ligand interactions: importance of integrating chemical and biological approaches.,Mahajan A, Yuan C, Pike BL, Heierhorst J, Chang CF, Tsai MD J Am Chem Soc. 2005 Oct 26;127(42):14572-3. PMID:16231900 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Protein kinase Spk1

spinqualitylabelsall models 2a0t, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image