eF-site ID 3hhd-ABCD PDB Code 3hhd Chain A, B, C, 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 A:  GEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRRW KAGLYGLPRRSGKLKDLSRFDASFFGVHPKQAHTMDPQLR LLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEAL SRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTA CSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQF LRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLAR RVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQSA GVAPESFEYIEAHGTGTKVGDPQELNGITRALCATRQEPL LIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFH SPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGSNV HIILRPNTQPPPAPAPHATLPRLLRASGRTPEAVQKLLEQ GLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGP EVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRDSI LRSDEAVKPFGLKVSQLLLSTDESTFDDIVHSFVSLTAIQ IGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAV LAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGVVP ACHNSKDTVTISGPQAPVFEFVEQLRKEGVFAKEVRTGGM AFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEA QWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLE IAPHALLQAVLKRGLKPSCTIIPLMKKDHRDNLEFFLAGI GRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDHSL AWDVPAAEDFPN B:  GEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRRW KAGLYGLPRRSGKLKDLSRFDASFFGVHPKQAHTMDPQLR LLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEAL SRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTA CSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSVQF LRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLAR RVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQSA GVAPESFEYIEAHGTGTKVGDPQELNGITRALCATRQEPL LIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFH SPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGSNV HIILRPNTQPPPAPAPHATLPRLLRASGRTPEAVQKLLEQ GLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGP EVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRDSI LRSDEAVKPFGLKVSQLLLSTDESTFDDIVHSFVSLTAIQ IGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAV LAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGVVP ACHNSKDTVTISGPQAPVFEFVEQLRKEGVFAKEVRTGGM AFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEA QWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLE IAPHALLQAVLKRGLKPSCTIIPLMKKDHRDNLEFFLAGI GRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDHSL AWDVPAAEDFPN C:  STGEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDR RWKAGLYGLPRRSGKLKDLSRFDASFFGVHPKQAHTMDPQ LRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSE ALSRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALD TACSSSLMALQNAYQAIHSGQCPAAIVGGINVLLKPNTSV QFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSL ARRVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQ SAGVAPESFEYIEAHGTGTKVGDPQELNGITRALCATRQE PLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLH FHSPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGS NVHIILRPNTQPPPAPAPHATLPRLLRASGRTPEAVQKLL EQGLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERG GPEVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRD SILRSDEAVKPFGLKVSQLLLSTDESTFDDIVHSFVSLTA IQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEE AVLAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGV VPACHNSKDTVTISGPQAPVFEFVEQLRKEGVFAKEVRTG GMAFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIP EAQWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVV LEIAPHALLQAVLKRGLKPSCTIIPLMKKDHRDNLEFFLA GIGRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDH SLAWDVPAAEDFPNG 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 C residue 589 type sequence Y description BINDING SITE FOR RESIDUE CL C 964 source : AC1 2) 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 3) chain B residue 207 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI7 4) 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 5) 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 6) chain A residue 725 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI8 7) chain B residue 725 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI8 8) chain C residue 725 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI8 9) chain D residue 725 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI8 10) chain A residue 63 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 11) chain B residue 63 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 12) chain C residue 63 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 13) chain D residue 63 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:23186163 source Swiss-Prot : SWS_FT_FI5 14) chain A residue 70 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 15) chain B residue 673 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 16) chain C residue 70 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 17) chain C residue 298 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 18) chain C residue 436 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 19) chain C residue 528 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 20) chain C residue 673 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 21) chain D residue 70 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 22) chain D residue 298 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 23) chain D residue 436 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 24) chain D residue 528 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 25) chain A residue 298 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 26) chain D residue 673 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 27) chain A residue 436 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 28) chain A residue 528 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 29) chain A residue 673 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 30) chain B residue 70 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 31) chain B residue 298 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 32) chain B residue 436 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 33) chain B residue 528 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 34) chain A residue 152-168 type prosite sequence GPSIALDTACSSSLMAL description KS3_1 Ketosynthase family 3 (KS3) active site signature. GPSiaLDtACSSSlmAL source prosite : PS00606 35) chain A residue 581 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU10022 source Swiss-Prot : SWS_FT_FI2 36) chain B residue 581 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU10022 source Swiss-Prot : SWS_FT_FI2 37) chain C residue 581 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU10022 source Swiss-Prot : SWS_FT_FI2 38) chain D residue 581 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000255|PROSITE-ProRule:PRU10022 source Swiss-Prot : SWS_FT_FI2 39) 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 40) 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 41) 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 42) 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 43) 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 44) 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 45) chain B residue 161 type ACT_SITE sequence C description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI1 46) chain B residue 293 type ACT_SITE sequence H description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI1 47) chain B residue 331 type ACT_SITE sequence H description For beta-ketoacyl synthase activity => ECO:0000255|PROSITE-ProRule:PRU01348 source Swiss-Prot : SWS_FT_FI1 48) 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 49) 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 50) 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 51) chain A residue 647 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4 52) chain D residue 647 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4 53) chain D residue 671 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4 54) chain D residue 773 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4 55) chain A residue 671 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4 56) chain A residue 773 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4 57) chain B residue 647 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4 58) chain B residue 671 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4 59) chain B residue 773 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4 60) chain C residue 647 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4 61) chain C residue 671 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4 62) chain C residue 773 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P19096 source Swiss-Prot : SWS_FT_FI4

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