4QFG

Structure of AMPK in complex with STAUROSPORINE inhibitor and in the absence of a synthetic activator

Summary for 4QFG

Related4QFS 4QFT
Descriptor5'-AMP-activated protein kinase catalytic subunit alpha-1, 5'-AMP-activated protein kinase subunit beta-1, 5'-AMP-activated protein kinase subunit gamma-1, ... (7 entities in total)
Functional Keywordscbm, kinase, ampk, signaling protein-inhibitor complex, signaling protein/inhibitor
Biological sourceRattus norvegicus (brown rat,rat,rats)
Cellular locationCytoplasm  P54645
Total number of polymer chains3
Total molecular weight119466.8
Authors
Calabrese, M.F.,Kurumbail, R.G. (deposition date: 2014-05-20, release date: 2014-08-06, Last modification date: 2017-11-22)
Primary citation
Calabrese, M.F.,Rajamohan, F.,Harris, M.S.,Caspers, N.L.,Magyar, R.,Withka, J.M.,Wang, H.,Borzilleri, K.A.,Sahasrabudhe, P.V.,Hoth, L.R.,Geoghegan, K.F.,Han, S.,Brown, J.,Subashi, T.A.,Reyes, A.R.,Frisbie, R.K.,Ward, J.,Miller, R.A.,Landro, J.A.,Londregan, A.T.,Carpino, P.A.,Cabral, S.,Smith, A.C.,Conn, E.L.,Cameron, K.O.,Qiu, X.,Kurumbail, R.G.
Structural Basis for AMPK Activation: Natural and Synthetic Ligands Regulate Kinase Activity from Opposite Poles by Different Molecular Mechanisms.
Structure, 22:1161-1172, 2014
PubMed: 25066137 (PDB entries with the same primary citation)
DOI: 10.1016/j.str.2014.06.009
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (3.46 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.26660.9%11.6%3.2%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation report