3HHD

Structure of the Human Fatty Acid Synthase KS-MAT Didomain as a Framework for Inhibitor Design.

Summary for 3HHD

DescriptorFatty acid synthase, CHLORIDE ION (3 entities in total)
Functional Keywordstransferase, fatty acid synthase, multienzyme, megasynthase, fatty acid synthesis, acetylation, cytoplasm, fatty acid biosynthesis, hydrolase, lipid synthesis, lyase, multifunctional enzyme, nad, nadp, oxidoreductase, phosphopantetheine, phosphoprotein, pyridoxal phosphate
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm  P49327
Total number of polymer chains4
Total molecular weight417979.59
Authors
Pappenberger, G.M.,Benz, J.,Thoma, R.,Rudolph, M.G. (deposition date: 2009-05-15, release date: 2010-02-09, Last modification date: 2017-11-01)
Primary citation
Pappenberger, G.,Benz, J.,Gsell, B.,Hennig, M.,Ruf, A.,Stihle, M.,Thoma, R.,Rudolph, M.G.
Structure of the human fatty acid synthase KS-MAT didomain as a framework for inhibitor design.
J.Mol.Biol., 397:508-519, 2010
PubMed: 20132826 (PDB entries with the same primary citation)
DOI: 10.1016/j.jmb.2010.01.066
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.15 Å)
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.21480.1%5.3%2.8%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution