eF-site ID 6ql9-B PDB Code 6ql9 Chain B 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 B:  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 B residue 335 type sequence H description binding site for residue EDO A 1911 source : AD2 2) chain B residue 342 type sequence Q description binding site for residue EDO A 1911 source : AD2 3) chain B residue 180 type sequence S description binding site for residue PNS B 1901 source : AE1 4) chain B residue 396 type sequence R description binding site for residue ACT B 1902 source : AE2 5) chain B residue 1358 type sequence H description binding site for residue ACT B 1902 source : AE2 6) chain B residue 1145 type sequence K description binding site for residue EDO B 1904 source : AE3 7) chain B residue 1153 type sequence D description binding site for residue EDO B 1904 source : AE3 8) chain B residue 1154 type sequence I description binding site for residue EDO B 1904 source : AE3 9) chain B residue 1004 type sequence I description binding site for residue EDO B 1905 source : AE4 10) chain B residue 1635 type sequence G description binding site for residue EDO B 1905 source : AE4 11) chain B residue 1636 type sequence V description binding site for residue EDO B 1905 source : AE4 12) chain B residue 1110 type sequence L description binding site for residue EDO B 1906 source : AE5 13) chain B residue 1111 type sequence F description binding site for residue EDO B 1906 source : AE5 14) chain B residue 1380 type sequence Q description binding site for residue EDO B 1906 source : AE5 15) chain B residue 1193 type sequence W description binding site for residue EDO B 1907 source : AE6 16) chain B residue 454 type sequence H description binding site for residue EDO B 1908 source : AE7 17) chain B residue 1573 type sequence I description binding site for residue EDO B 1908 source : AE7 18) chain B residue 1635 type sequence G description binding site for residue EDO B 1908 source : AE7 19) chain B residue 1057 type sequence M description binding site for residue EDO B 1909 source : AE8 20) chain B residue 1059 type sequence F description binding site for residue EDO B 1909 source : AE8 21) chain B residue 1100 type sequence H description binding site for residue EDO B 1909 source : AE8 22) chain B residue 1206 type sequence S description binding site for residue EDO B 1910 source : AE9 23) chain B residue 1208 type sequence V description binding site for residue EDO B 1910 source : AE9 24) chain B residue 1271 type sequence Q description binding site for residue EDO B 1910 source : AE9 25) chain B residue 1251 type sequence M description binding site for residue EDO B 1911 source : AF1 26) chain B residue 1278 type sequence S description binding site for residue EDO B 1911 source : AF1 27) chain B residue 1197 type sequence T description binding site for residue EDO B 1912 source : AF2 28) chain B residue 985 type sequence R description binding site for residue NA B 1913 source : AF3 29) chain B residue 1048 type sequence E description binding site for residue NA B 1913 source : AF3 30) chain B residue 1252 type sequence G description binding site for residue NA B 1914 source : AF4 31) chain B residue 1254 type sequence V description binding site for residue NA B 1914 source : AF4 32) chain B residue 1333 type sequence D description binding site for residue NA B 1914 source : AF4 33) chain B residue 1334 type sequence D description binding site for residue NA B 1914 source : AF4 34) chain B residue 1513 type sequence Y description binding site for residue NA B 1915 source : AF5 35) chain B residue 1514 type sequence K description binding site for residue NA B 1915 source : AF5 36) chain B residue 1516 type sequence D description binding site for residue NA B 1915 source : AF5 37) chain B residue 1519 type sequence I description binding site for residue NA B 1915 source : AF5 38) chain B residue 1540 type sequence S description binding site for residue NA B 1916 source : AF6 39) chain B residue 1541 type sequence F description binding site for residue NA B 1916 source : AF6 40) chain B residue 1575 type sequence V description binding site for residue NA B 1916 source : AF6 41) chain B residue 1577 type sequence Q description binding site for residue NA B 1916 source : AF6 42) chain B residue 1592 type sequence M description binding site for residue NA B 1916 source : AF6 43) chain B residue 1209 type sequence D description binding site for residue NA B 1917 source : AF7 44) chain B residue 1212 type sequence T description binding site for residue NA B 1917 source : AF7 45) chain B residue 1277 type sequence E description binding site for residue NA B 1917 source : AF7 46) chain B residue 682 type sequence G description binding site for residue A2P B 1918 source : AF8 47) chain B residue 684 type sequence G description binding site for residue A2P B 1918 source : AF8 48) chain B residue 707 type sequence T description binding site for residue A2P B 1918 source : AF8 49) chain B residue 708 type sequence S description binding site for residue A2P B 1918 source : AF8 50) chain B residue 709 type sequence R description binding site for residue A2P B 1918 source : AF8 51) chain B residue 738 type sequence N description binding site for residue A2P B 1918 source : AF8 52) chain B residue 739 type sequence Q description binding site for residue A2P B 1918 source : AF8 53) chain B residue 773 type sequence A description binding site for residue A2P B 1918 source : AF8 54) chain B residue 774 type sequence I description binding site for residue A2P B 1918 source : AF8 55) chain B residue 854 type sequence H description binding site for residue EDO E 1909 source : AL1 56) chain B residue 1305 type sequence C description binding site for Di-peptide PNS E 1901 and SER E 180 source : AQ5 57) chain B residue 1346 type sequence M description binding site for Di-peptide PNS E 1901 and SER E 180 source : AQ5 58) chain B residue 1417 type sequence S description binding site for Di-peptide PNS E 1901 and SER E 180 source : AQ5 59) chain B residue 1419 type sequence P description binding site for Di-peptide PNS E 1901 and SER E 180 source : AQ5 60) chain B residue 1420 type sequence A description binding site for Di-peptide PNS E 1901 and SER E 180 source : AQ5 61) chain B residue 1542 type sequence H description binding site for Di-peptide PNS E 1901 and SER E 180 source : AQ5 62) chain B residue 1544 type sequence T description binding site for Di-peptide PNS E 1901 and SER E 180 source : AQ5 63) chain B residue 1546 type sequence T description binding site for Di-peptide PNS E 1901 and SER E 180 source : AQ5 64) chain B residue 1549 type sequence N description binding site for Di-peptide PNS E 1901 and SER E 180 source : AQ5 65) chain B residue 1644 type sequence F description binding site for Di-peptide PNS E 1901 and SER E 180 source : AQ5 66) chain B residue 1646 type sequence F description binding site for Di-peptide PNS E 1901 and SER E 180 source : AQ5 67) chain B residue 958 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 68) chain B residue 1440 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 69) chain B residue 1542 type ACT_SITE sequence H description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 70) chain B residue 1583 type ACT_SITE sequence H description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 71) chain B residue 1773 type ACT_SITE sequence V description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 72) chain B residue 1774 type ACT_SITE sequence E description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 73) chain B residue 1817 type ACT_SITE sequence E description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 74) chain B residue 1841 type ACT_SITE sequence R description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 75) chain B residue 1871 type ACT_SITE sequence I description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 76) chain B residue 1872 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 77) chain B residue 1873 type ACT_SITE sequence H description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 78) chain B residue 1772 type ACT_SITE sequence D description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 79) chain B 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 80) chain B 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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