Human AMP-activated protein kinase alpha 2 subunit kinase domain (T172D) complexed with compound C

Summary for 3AQV

Related2yza 2h6d
Descriptor5'-AMP-activated protein kinase catalytic subunit alpha-2, 6-[4-(2-piperidin-1-ylethoxy)phenyl]-3-pyridin-4-ylpyrazolo[1,5-a]pyrimidine (3 entities in total)
Functional Keywordsstructural genomics, riken structural genomics/proteomics initiative, rsgi, transferase, signaling protein, serine/threonine protein kinase, phosphorylation, atp-binding, nucleotide-binding, cholesterol biosynthesis, fatty acid biosynthesis, lipid synthesis, glucose metabolism, magnesium, metal-binding, serine/threonine-protein kinase, steroid biosynthesis, transferase-transferase inhibitor complex, transferase/transferase inhibitor
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm (By similarity) P54646
Total number of polymer chains1
Total molecular weight31971.22
Handa, N.,Takagi, T.,Saijo, S.,Kishishita, S.,Toyama, M.,Terada, T.,Shirouzu, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2010-11-19, release date: 2011-04-27, Last modification date: 2012-04-11)
Primary citation
Handa, N.,Takagi, T.,Saijo, S.,Kishishita, S.,Takaya, D.,Toyama, M.,Terada, T.,Shirouzu, M.,Suzuki, A.,Lee, S.,Yamauchi, T.,Okada-Iwabu, M.,Iwabu, M.,Kadowaki, T.,Minokoshi, Y.,Yokoyama, S.
Structural basis for compound C inhibition of the human AMP-activated protein kinase alpha 2 subunit kinase domain
Acta Crystallogr.,Sect.D, 67:480-487, 2011
PubMed: 21543851 (PDB entries with the same primary citation)
DOI: 10.1107/S0907444911010201
MImport into Mendeley
Experimental method

Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers 0.26833 1.5% 6.8% 15.0%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
PDB entries from 2020-10-21