eF-site ID 6ql9-F PDB Code 6ql9 Chain F click to enlarge Title Structure of Fatty acid synthase complex from Saccharomyces cerevisiae at 2.9 Angstrom Classification TRANSFERASE Compound Fatty acid synthase subunit alpha Source ORGANISM_COMMON: Baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae (strain ATCC 204508 / S288c); Sequence F:  MKPEVEQELAHILLTELLAYQFASPVRWIETQDVFLKDFN TERVVEIGPSPTLAGMAQRTLKNKYESYDAALSLHREILC YSKDAKEIYYTPDPSEIADEPVKASLLLHVLVAHKLKKSL DSIPMSKTIKDLVGGKSTVQNEILGDLGKEFGTTPEKPEE TPLEELAETFQDTFSGALGKQSSSLLSRLISSKMPGGFTI TVARKYLQTRWGLPSGRQDGVLLVALSNEPAARLGSEADA KAFLDSMAQKYASIVGVDLLEEITKDHKVLARQQLQVLAR YLKMDLDNGERKFLKEKDTVAELQAQLDYLNAELGEFFVN GVATSFSRKKARTFDSSWNWAKQSLLSLYFEIIHGVLKNV DREVVSEAINIMNRSNDALIKFMEYHISNTDETKGENYQL VKTLGEQLIENCKQVLDVDPVYKDVAKPTGPKTAIDKNGN ITYSEEPREKVRKLSQYVQEMALGGPITKESMDVEDALDK DSTKEVASLPNKSTISKTVSSTIPRETIPFLHLRKKTPAG DWKYDRQLSSLFLDGLEKAAFNGVTFKDKYVLITGAGKGS IGAEVLQGLLQGGAKVVVTTSRFSKQVTDYYQSIYAKYGA KGSTLIVVPFNQGSKQDVEALIEFIYDTEKNGGLGWDLDA IIPFAAIPEQGIELEHIDSKSEFAHRIMLTNILRMMGCVK KQKSARGIETRPAQVILPMSPNHGTFGGDGMYSESKLSLE TLFNRWHSESWANQLTVCGAIIGWTRGTGLMSANNIIAEG IEKMGVRTFSQKEMAFNLLGLLTPEVVELCQKSPVMADLN GGLQFVPELKEFTAKLRKELVETSEVRKAVSIETALEHKV VNGNSADAAYAQVEIQPRANIQLDFPELKPYKQVKQIAPA ELEGLLDLERVIVVTGFAEVGPWGSARTRWEMEAFGEFSL EGCVEMAWIMGFISYHNGNLKGRPYTGWVDSKTKEPVDDK DVKAKYETSILEHSGIRLIEPELFNGYNPEKKEMIQEVIV EEDLEPFEASKETAEQFKHQHGDKVDIFEIPETGEYSVKL LKGATLYIPKALRFDRLVAGQIPTGWNAKTYGISDDIISQ VDPITLFVLVSVVEAFIASGITDPYEMYKYVHVSEVGNCS GSGMGGVSALRGMFKDRFKDEPVQNDILQESFINTMSAWV NMLLISSSGPIKTPVGACATSVESVDIGVETILSGKARIC IVGGYDDFQEEGSFEFGNMKATSNTLEEFEHGRTPAEMSR PATTTRNGFMEAQGAGIQIIMQADLALKMGVPIYGIVAMA ATATDKIGRSVPAPGKGILTTAREHHSSVKYASPNLNMKY RKRQLVTREAQIKDWVENELEALKLEAEEIPSEDQNEFLL ERTREIHNEAESQLRAAQQQWGNDFYKRDPRIAPLRGALA TYGLTIDDLGVASFHGTSTKANDKNESATINEMMKHLGRS EGNPVIGVFQKFLTGHPKGAAGAWMMNGALQILNSGIIPG NRNADNVDKILEQFEYVLYPSKTLKTDGVRAVSITSFGFG QKGGQAIVVHPDYLYGAITEDRYNEYVAKVSAREKSAYKF FHNGMIYNKLFVSKEHAPYTDELEEDVYLDPLARVSKDKK SGSLTFNSKNIQSKDSYINANTIETAKMIENMTKEKVSNG GVGVDVELITSINVENDTFIERNFTPQEIEYCSAQPSVQS SFAGTWSAKEAVFKSLGVKSLGGGAALKDIEIVRVNKNAP AVELHGNAKKAAEEAGVTDVKVSISHDDLQAVAVAVSTK Description Functional site 1) chain F residue 1305 type sequence C description binding site for residue PNS A 1901 source : AC1 2) chain F residue 1346 type sequence M description binding site for residue PNS A 1901 source : AC1 3) chain F residue 1417 type sequence S description binding site for residue PNS A 1901 source : AC1 4) chain F residue 1419 type sequence P description binding site for residue PNS A 1901 source : AC1 5) chain F residue 1420 type sequence A description binding site for residue PNS A 1901 source : AC1 6) chain F residue 1542 type sequence H description binding site for residue PNS A 1901 source : AC1 7) chain F residue 1544 type sequence T description binding site for residue PNS A 1901 source : AC1 8) chain F residue 1546 type sequence T description binding site for residue PNS A 1901 source : AC1 9) chain F residue 1549 type sequence N description binding site for residue PNS A 1901 source : AC1 10) chain F residue 1583 type sequence H description binding site for residue PNS A 1901 source : AC1 11) chain F residue 1644 type sequence F description binding site for residue PNS A 1901 source : AC1 12) chain F residue 1646 type sequence F description binding site for residue PNS A 1901 source : AC1 13) chain F residue 854 type sequence H description binding site for residue EDO A 1908 source : AC8 14) chain F residue 1251 type sequence M description binding site for residue EDO C 1911 source : AH1 15) chain F residue 1278 type sequence S description binding site for residue EDO C 1911 source : AH1 16) chain F residue 335 type sequence H description binding site for residue EDO E 1910 source : AL2 17) chain F residue 398 type sequence K description binding site for residue EDO F 1902 source : AM2 18) chain F residue 1004 type sequence I description binding site for residue EDO F 1903 source : AM3 19) chain F residue 1635 type sequence G description binding site for residue EDO F 1903 source : AM3 20) chain F residue 1194 type sequence N description binding site for residue EDO F 1904 source : AM4 21) chain F residue 401 type sequence T description binding site for residue EDO F 1905 source : AM5 22) chain F residue 759 type sequence G description binding site for residue EDO F 1905 source : AM5 23) chain F residue 760 type sequence G description binding site for residue EDO F 1905 source : AM5 24) chain F residue 764 type sequence D description binding site for residue EDO F 1906 source : AM6 25) chain F residue 818 type sequence R description binding site for residue EDO F 1906 source : AM6 26) chain F residue 1223 type sequence F description binding site for residue EDO F 1907 source : AM7 27) chain F residue 1228 type sequence I description binding site for residue EDO F 1907 source : AM7 28) chain F residue 1229 type sequence T description binding site for residue EDO F 1907 source : AM7 29) chain F residue 1231 type sequence P description binding site for residue EDO F 1907 source : AM7 30) chain F residue 1697 type sequence L description binding site for residue EDO F 1907 source : AM7 31) chain F residue 1178 type sequence A description binding site for residue EDO F 1908 source : AM8 32) chain F residue 1180 type sequence R description binding site for residue EDO F 1908 source : AM8 33) chain F residue 1110 type sequence L description binding site for residue EDO F 1909 source : AM9 34) chain F residue 1189 type sequence I description binding site for residue EDO F 1909 source : AM9 35) chain F residue 1214 type sequence F description binding site for residue EDO F 1909 source : AM9 36) chain F residue 1380 type sequence Q description binding site for residue EDO F 1909 source : AM9 37) chain F residue 1026 type sequence E description binding site for residue NA F 1910 source : AN1 38) chain F residue 1028 type sequence G description binding site for residue NA F 1910 source : AN1 39) chain F residue 1036 type sequence R description binding site for residue NA F 1910 source : AN1 40) chain F residue 615 type sequence S description binding site for residue NA F 1911 source : AN2 41) chain F residue 618 type sequence N description binding site for residue NA F 1911 source : AN2 42) chain F residue 620 type sequence S description binding site for residue NA F 1911 source : AN2 43) chain F residue 668 type sequence F description binding site for residue NA F 1911 source : AN2 44) chain F residue 682 type sequence G description binding site for residue A2P F 1912 source : AN3 45) chain F residue 684 type sequence G description binding site for residue A2P F 1912 source : AN3 46) chain F residue 706 type sequence T description binding site for residue A2P F 1912 source : AN3 47) chain F residue 707 type sequence T description binding site for residue A2P F 1912 source : AN3 48) chain F residue 708 type sequence S description binding site for residue A2P F 1912 source : AN3 49) chain F residue 738 type sequence N description binding site for residue A2P F 1912 source : AN3 50) chain F residue 739 type sequence Q description binding site for residue A2P F 1912 source : AN3 51) chain F residue 772 type sequence A description binding site for residue A2P F 1912 source : AN3 52) chain F residue 773 type sequence A description binding site for residue A2P F 1912 source : AN3 53) chain F residue 774 type sequence I description binding site for residue A2P F 1912 source : AN3 54) chain F residue 794 type sequence I description binding site for residue A2P F 1912 source : AN3 55) chain F residue 178 type sequence G description binding site for Di-peptide PNS F 1901 and SER F 180 source : AQ6 56) chain F residue 179 type sequence K description binding site for Di-peptide PNS F 1901 and SER F 180 source : AQ6 57) chain F residue 181 type sequence T description binding site for Di-peptide PNS F 1901 and SER F 180 source : AQ6 58) chain F residue 182 type sequence V description binding site for Di-peptide PNS F 1901 and SER F 180 source : AQ6 59) chain F residue 183 type sequence Q description binding site for Di-peptide PNS F 1901 and SER F 180 source : AQ6 60) chain F residue 184 type sequence N description binding site for Di-peptide PNS F 1901 and SER F 180 source : AQ6 61) chain F residue 958 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 62) chain F residue 1440 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 63) chain F residue 1305 type ACT_SITE sequence C description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 64) chain F residue 1542 type ACT_SITE sequence H description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 65) chain F residue 1583 type ACT_SITE sequence H description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 66) chain F residue 1772 type ACT_SITE sequence D description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 67) chain F residue 1773 type ACT_SITE sequence V description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 68) chain F residue 1774 type ACT_SITE sequence E description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 69) chain F residue 1817 type ACT_SITE sequence E description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 70) chain F residue 1841 type ACT_SITE sequence R description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 71) chain F residue 1871 type ACT_SITE sequence I description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 72) chain F residue 1872 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 73) chain F residue 1873 type ACT_SITE sequence H description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 74) chain F residue 1798 type MOD_RES sequence Y description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI3 75) chain F residue 1808 type MOD_RES sequence S description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI3 76) chain F residue 50 type MOD_RES sequence S description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI4 77) chain F residue 180 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 78) chain F residue 523 type CROSSLNK sequence S description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI6 79) chain F residue 37 type CROSSLNK sequence K description Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047 source Swiss-Prot : SWS_FT_FI8

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