4QFR

Structure of AMPK in complex with Cl-A769662 activator and STAUROSPORINE inhibitor

Summary for 4QFR

Related4QFG 4QFS
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, ... (9 entities in total)
Functional Keywordscbm, ampk, kinase, signaling protein-inhibitor-activator complex, signaling protein/inhibitor/activator
Biological sourceRattus norvegicus (brown rat,rat,rats)
Cellular locationCytoplasm  P54645
Total number of polymer chains3
Total molecular weight120514.84
Authors
Calabrese, M.F.,Kurumbail, R.G. (deposition date: 2014-05-21, 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 (3.34 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.24880.6%7.9%3.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution