Entry Database : PDB / ID : 6nna Structure visualization Downloads & linksTitle Human Fatty Acid Synthase Psi/KR Tri-Domain with NADPH and Compound 22 ComponentsFatty acid synthase,Fatty acid synthase Details Keywords TRANSFERASE / FATTY ACID SYNTHASE / HUMAN FAS / KETO-REDUCTASEFunction / homology Function and homology informationFunction Domain/homology Component
fatty-acid synthase system / ether lipid biosynthetic process / Vitamin B5 (pantothenate) metabolism / neutrophil differentiation / [acyl-carrier-protein] S-acetyltransferase / enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) / [acyl-carrier-protein] S-acetyltransferase activity / glandular epithelial cell development / enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity / oleoyl-[acyl-carrier-protein] hydrolase ... fatty-acid synthase system / ether lipid biosynthetic process / Vitamin B5 (pantothenate) metabolism / neutrophil differentiation / [acyl-carrier-protein] S-acetyltransferase / enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific) / [acyl-carrier-protein] S-acetyltransferase activity / glandular epithelial cell development / enoyl-[acyl-carrier-protein] reductase (NADPH, A-specific) activity / oleoyl-[acyl-carrier-protein] hydrolase / oleoyl-[acyl-carrier-protein] hydrolase activity / myristoyl-[acyl-carrier-protein] hydrolase activity / palmitoyl-[acyl-carrier-protein] hydrolase activity / fatty acid synthase activity / glycogen granule / Fatty acyl-CoA biosynthesis / establishment of endothelial intestinal barrier / ChREBP activates metabolic gene expression / [acyl-carrier-protein] S-malonyltransferase / [acyl-carrier-protein] S-malonyltransferase activity / modulation by host of viral process / 3-hydroxyacyl-[acyl-carrier-protein] dehydratase / (3R)-hydroxymyristoyl-[acyl-carrier-protein] dehydratase activity / (3R)-3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase activity / (3R)-3-hydroxyoctanoyl-[acyl-carrier-protein] dehydratase activity / (3R)-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity / beta-ketoacyl-[acyl-carrier-protein] synthase I / NR1H2 & NR1H3 regulate gene expression linked to lipogenesis / 3-oxoacyl-[acyl-carrier-protein] reductase / 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity / mammary gland development / phosphopantetheine binding / 3-oxoacyl-[acyl-carrier-protein] synthase activity / monocyte differentiation / cellular response to interleukin-4 / fatty acid metabolic process / Activation of gene expression by SREBF (SREBP) / osteoblast differentiation / fatty acid biosynthetic process / melanosome / cadherin binding / inflammatory response / Golgi apparatus / RNA binding / extracellular exosome / membrane / plasma membrane / cytosol / cytoplasm Similarity search - Function Methyltransferase type 12 / Methyltransferase domain / Thioesterase / Thioesterase domain / PKS_DH / Polyketide synthase, dehydratase domain superfamily / Polyketide synthase, dehydratase domain / Polyketide synthase dehydratase / Ketosynthase family 3 (KS3) domain profile. / Polyketide synthase, ketoreductase domain ... Methyltransferase type 12 / Methyltransferase domain / Thioesterase / Thioesterase domain / PKS_DH / Polyketide synthase, dehydratase domain superfamily / Polyketide synthase, dehydratase domain / Polyketide synthase dehydratase / Ketosynthase family 3 (KS3) domain profile. / Polyketide synthase, ketoreductase domain / KR domain / Malonyl-CoA ACP transacylase, ACP-binding / Polyketide synthase, C-terminal extension / Ketoacyl-synthetase C-terminal extension / PKS_KR / Acyl transferase domain superfamily / Acyl transferase / Acyl transferase domain / Acyl transferase domain in polyketide synthase (PKS) enzymes. / Acyl transferase/acyl hydrolase/lysophospholipase / Alcohol dehydrogenase-like, C-terminal / Zinc-binding dehydrogenase / Beta-ketoacyl synthase, active site / Ketosynthase family 3 (KS3) active site signature. / Polyketide synthase, beta-ketoacyl synthase domain / Beta-ketoacyl synthase / Polyketide synthase, enoylreductase domain / Enoylreductase / Polyketide synthase, phosphopantetheine-binding domain / Phosphopantetheine attachment site / Beta-ketoacyl synthase, N-terminal / Beta-ketoacyl synthase, C-terminal / Beta-ketoacyl synthase, N-terminal domain / Beta-ketoacyl synthase, C-terminal domain / GroES-like superfamily / Thiolase-like / Phosphopantetheine attachment site / Phosphopantetheine attachment site. / Phosphopantetheine attachment site / ACP-like superfamily / Carrier protein (CP) domain profile. / Phosphopantetheine binding ACP domain / Alpha/Beta hydrolase fold / NAD(P)-binding Rossmann-like Domain / S-adenosyl-L-methionine-dependent methyltransferase superfamily / NAD(P)-binding domain superfamily / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta Similarity search - Domain/homologyBiological species Homo sapiens (human)Method X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution : 2.26 Å DetailsAuthors Toms, A.V. / Martin, M.W. CitationJournal : Bioorg. Med. Chem. Lett. / Year : 2019Title : Discovery and optimization of novel piperazines as potent inhibitors of fatty acid synthase (FASN).Authors: Martin, M.W. / Lancia Jr., D.R. / Li, H. / Schiller, S.E.R. / Toms, A.V. / Wang, Z. / Bair, K.W. / Castro, J. / Fessler, S. / Gotur, D. / Hubbs, S.E. / Kauffman, G.S. / Kershaw, M. / Luke, G. ... Authors : Martin, M.W. / Lancia Jr., D.R. / Li, H. / Schiller, S.E.R. / Toms, A.V. / Wang, Z. / Bair, K.W. / Castro, J. / Fessler, S. / Gotur, D. / Hubbs, S.E. / Kauffman, G.S. / Kershaw, M. / Luke, G.P. / McKinnon, C. / Yao, L. / Lu, W. / Millan, D.S. History Deposition Jan 14, 2019 Deposition site : RCSB / Processing site : RCSBRevision 1.0 Feb 20, 2019 Provider : repository / Type : Initial releaseRevision 1.1 Mar 13, 2019 Group : Data collection / Database references / Category : citation / citation_author / pdbx_database_procItem : _citation.journal_abbrev / _citation.pdbx_database_id_PubMed ... _citation.journal_abbrev / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name Revision 1.2 Mar 20, 2019 Group : Data collection / Database references / Category : citationItem : _citation.journal_volume / _citation.page_first / _citation.page_last
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