eF-site ID 3hhd-C PDB Code 3hhd Chain C 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 null (FAS_HUMAN) Sequence C:  STGEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDR RWKAGLYGLPRRSGKLKDLSRFDASFFGVHPKQAHTMDPQ LRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSE ALSRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALD TACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSV QFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSL ARRVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQ SAGVAPESFEYIEAHGTGTKVGDPQELNGITRALCATRQE PLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLH FHSPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGS NVHIILRPNTQPPPAPAPHATLPRLLRASGRTPEAVQKLL EQGLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERG GPEVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRD SILRSDEAVKPFGLKVSQLLLSTDESTFDDIVHSFVSLTA IQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEE AVLAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGV VPACHNSKDTVTISGPQAPVFEFVEQLRKEGVFAKEVRTG GMAFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIP EAQWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVV LEIAPHALLQAVLKRGLKPSCTIIPLMKKDHRDNLEFFLA GIGRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDH SLAWDVPAAEDFPNG Description Functional site 1) chain C residue 589 type sequence Y description BINDING SITE FOR RESIDUE CL C 964 source : AC1 2) chain C residue 207 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 3) chain C residue 725 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI8 4) chain C residue 161 type ACT_SITE sequence C description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI1 5) chain C residue 293 type ACT_SITE sequence H description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI1 6) chain C residue 331 type ACT_SITE sequence H description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI1 7) chain C residue 581 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU10022 source Swiss-Prot : SWS_FT_FI2 8) chain C residue 773 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4 9) chain C residue 647 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4 10) chain C residue 671 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4 11) chain C residue 63 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 12) chain C residue 70 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 13) chain C residue 298 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 14) chain C residue 436 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 15) chain C residue 528 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 16) chain C residue 673 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6

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