eF-site ID 3hhd-D PDB Code 3hhd Chain D click to enlarge Title Structure of the Human Fatty Acid Synthase KS-MAT Didomain as a Framework for Inhibitor Design. Classification Transferase, Hydrolase Compound Fatty acid synthase Source Homo sapiens (Human) (FAS_HUMAN) Sequence D:  STGEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDR RWKAGLYGLPRRSGKLKDLSRFDASFFGVHPKQAHTMDPQ LRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSE ALSRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALD TACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSV QFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSL ARRVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQ SAGVAPESFEYIEAHGTGTKVGDPQELNGITRALCATRQE PLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLH FHSPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGS NVHIILRPNTQPPPAPAPHATLPRLLRASGRTPEAVQKLL EQGLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERG GPEVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRD SILRSDEAVKPFGLKVSQLLLSTDESTFDDIVHSFVSLTA IQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEE AVLAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGV VPACHNSKDTVTISGPQAPVFEFVEQLRKEGVFAKEVRTG GMAFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIP EAQWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVV LEIAPHALLQAVLKRGLKPSCTIIPLMKKDHRDNLEFFLA GIGRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDH SLAWDVPAAEDFPN Description Functional site 1) chain D residue 161 type ACT_SITE sequence C description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI1 2) chain D residue 293 type ACT_SITE sequence H description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI1 3) chain D residue 331 type ACT_SITE sequence H description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI1 4) chain D residue 581 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU10022 source Swiss-Prot : SWS_FT_FI2 5) chain D residue 647 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4 6) chain D residue 671 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4 7) chain D residue 773 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4 8) chain D residue 63 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 9) chain D residue 70 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 10) chain D residue 298 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 11) chain D residue 436 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 12) chain D residue 528 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 13) chain D residue 673 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 14) chain D residue 207 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 15) chain D residue 725 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI8

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