3HHD
Structure of the Human Fatty Acid Synthase KS-MAT Didomain as a Framework for Inhibitor Design.
Summary for 3HHD
| Entry DOI | 10.2210/pdb3hhd/pdb |
| Descriptor | Fatty acid synthase, CHLORIDE ION (3 entities in total) |
| Functional Keywords | transferase, 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 source | Homo sapiens (human) |
| Cellular location | Cytoplasm : P49327 |
| Total number of polymer chains | 4 |
| Total formula weight | 417979.59 |
| Authors | Pappenberger, G.M.,Benz, J.,Thoma, R.,Rudolph, M.G. (deposition date: 2009-05-15, release date: 2010-02-09, Last modification date: 2023-09-06) |
| 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 Cited by PubMed: 20132826DOI: 10.1016/j.jmb.2010.01.066 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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