eF-site ID 3hhd-A PDB Code 3hhd Chain A 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 A:  GEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRRW KAGLYGLPRRSGKLKDLSRFDASFFGVHPKQAHTMDPQLR LLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEAL SRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTA CSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQF LRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLAR RVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQSA GVAPESFEYIEAHGTGTKVGDPQELNGITRALCATRQEPL LIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFH SPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGSNV HIILRPNTQPPPAPAPHATLPRLLRASGRTPEAVQKLLEQ GLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGP EVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRDSI LRSDEAVKPFGLKVSQLLLSTDESTFDDIVHSFVSLTAIQ IGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAV LAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGVVP ACHNSKDTVTISGPQAPVFEFVEQLRKEGVFAKEVRTGGM AFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEA QWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLE IAPHALLQAVLKRGLKPSCTIIPLMKKDHRDNLEFFLAGI GRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDHSL AWDVPAAEDFPN Description Functional site 1) chain A residue 207 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 2) chain A residue 725 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI8 3) chain A residue 63 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 4) chain A residue 70 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 5) chain A residue 298 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 6) chain A residue 436 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 7) chain A residue 528 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 8) chain A residue 673 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 9) chain A residue 152-168 type prosite sequence GPSIALDTACSSSLMAL description KS3_1 Ketosynthase family 3 (KS3) active site signature. GPSiaLDtACSSSlmAL source prosite : PS00606 10) chain A residue 581 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU10022 source Swiss-Prot : SWS_FT_FI2 11) chain A residue 161 type ACT_SITE sequence C description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 293 type ACT_SITE sequence H description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI1 13) chain A residue 331 type ACT_SITE sequence H description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 647 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4 15) chain A residue 671 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4 16) chain A residue 773 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4

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