eF-site ID 6ql9-C PDB Code 6ql9 Chain C 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 C:  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 C residue 342 type sequence Q description binding site for residue EDO A 1911 source : AD2 2) chain C residue 359 type sequence R description binding site for residue EDO B 1904 source : AE3 3) chain C residue 180 type sequence S description binding site for residue PNS C 1901 source : AF9 4) chain C residue 184 type sequence N description binding site for residue PNS C 1901 source : AF9 5) chain C residue 1635 type sequence G description binding site for residue ACT C 1902 source : AG1 6) chain C residue 1660 type sequence Y description binding site for residue ACT C 1902 source : AG1 7) chain C residue 440 type sequence M description binding site for residue ACT C 1903 source : AG2 8) chain C residue 491 type sequence K description binding site for residue ACT C 1903 source : AG2 9) chain C residue 616 type sequence L description binding site for residue ACT C 1903 source : AG2 10) chain C residue 454 type sequence H description binding site for residue EDO C 1904 source : AG3 11) chain C residue 1635 type sequence G description binding site for residue EDO C 1904 source : AG3 12) chain C residue 1110 type sequence L description binding site for residue EDO C 1905 source : AG4 13) chain C residue 1111 type sequence F description binding site for residue EDO C 1905 source : AG4 14) chain C residue 1189 type sequence I description binding site for residue EDO C 1905 source : AG4 15) chain C residue 1380 type sequence Q description binding site for residue EDO C 1905 source : AG4 16) chain C residue 1191 type sequence T description binding site for residue EDO C 1906 source : AG5 17) chain C residue 1206 type sequence S description binding site for residue EDO C 1907 source : AG6 18) chain C residue 1208 type sequence V description binding site for residue EDO C 1907 source : AG6 19) chain C residue 1271 type sequence Q description binding site for residue EDO C 1907 source : AG6 20) chain C residue 809 type sequence Q description binding site for residue EDO C 1908 source : AG7 21) chain C residue 643 type sequence K description binding site for residue EDO C 1909 source : AG8 22) chain C residue 851 type sequence N description binding site for residue EDO C 1909 source : AG8 23) chain C residue 1360 type sequence R description binding site for residue EDO C 1910 source : AG9 24) chain C residue 1361 type sequence T description binding site for residue EDO C 1910 source : AG9 25) chain C residue 1251 type sequence M description binding site for residue EDO C 1911 source : AH1 26) chain C residue 1278 type sequence S description binding site for residue EDO C 1911 source : AH1 27) chain C residue 1428 type sequence T description binding site for residue EDO C 1912 source : AH2 28) chain C residue 1430 type sequence R description binding site for residue EDO C 1912 source : AH2 29) chain C residue 985 type sequence R description binding site for residue NA C 1913 source : AH3 30) chain C residue 1048 type sequence E description binding site for residue NA C 1913 source : AH3 31) chain C residue 1026 type sequence E description binding site for residue NA C 1914 source : AH4 32) chain C residue 1028 type sequence G description binding site for residue NA C 1914 source : AH4 33) chain C residue 1036 type sequence R description binding site for residue NA C 1914 source : AH4 34) chain C residue 1034 type sequence R description binding site for residue NA C 1915 source : AH5 35) chain C residue 1052 type sequence E description binding site for residue NA C 1915 source : AH5 36) chain C residue 1198 type sequence Y description binding site for residue NA C 1915 source : AH5 37) chain C residue 1221 type sequence E description binding site for residue NA C 1915 source : AH5 38) chain C residue 1209 type sequence D description binding site for residue NA C 1916 source : AH6 39) chain C residue 1212 type sequence T description binding site for residue NA C 1916 source : AH6 40) chain C residue 1277 type sequence E description binding site for residue NA C 1916 source : AH6 41) chain C residue 1283 type sequence M description binding site for residue NA C 1916 source : AH6 42) chain C residue 682 type sequence G description binding site for residue A2P C 1917 source : AH7 43) chain C residue 684 type sequence G description binding site for residue A2P C 1917 source : AH7 44) chain C residue 687 type sequence S description binding site for residue A2P C 1917 source : AH7 45) chain C residue 707 type sequence T description binding site for residue A2P C 1917 source : AH7 46) chain C residue 708 type sequence S description binding site for residue A2P C 1917 source : AH7 47) chain C residue 737 type sequence F description binding site for residue A2P C 1917 source : AH7 48) chain C residue 738 type sequence N description binding site for residue A2P C 1917 source : AH7 49) chain C residue 739 type sequence Q description binding site for residue A2P C 1917 source : AH7 50) chain C residue 772 type sequence A description binding site for residue A2P C 1917 source : AH7 51) chain C residue 773 type sequence A description binding site for residue A2P C 1917 source : AH7 52) chain C residue 774 type sequence I description binding site for residue A2P C 1917 source : AH7 53) chain C residue 1142 type sequence E description binding site for residue EDO F 1908 source : AM8 54) chain C residue 1146 type sequence H description binding site for residue EDO F 1908 source : AM8 55) chain C residue 1305 type sequence C description binding site for Di-peptide PNS D 1901 and SER D 180 source : AQ4 56) chain C residue 1346 type sequence M description binding site for Di-peptide PNS D 1901 and SER D 180 source : AQ4 57) chain C residue 1417 type sequence S description binding site for Di-peptide PNS D 1901 and SER D 180 source : AQ4 58) chain C residue 1419 type sequence P description binding site for Di-peptide PNS D 1901 and SER D 180 source : AQ4 59) chain C residue 1420 type sequence A description binding site for Di-peptide PNS D 1901 and SER D 180 source : AQ4 60) chain C residue 1542 type sequence H description binding site for Di-peptide PNS D 1901 and SER D 180 source : AQ4 61) chain C residue 1544 type sequence T description binding site for Di-peptide PNS D 1901 and SER D 180 source : AQ4 62) chain C residue 1546 type sequence T description binding site for Di-peptide PNS D 1901 and SER D 180 source : AQ4 63) chain C residue 1548 type sequence A description binding site for Di-peptide PNS D 1901 and SER D 180 source : AQ4 64) chain C residue 1549 type sequence N description binding site for Di-peptide PNS D 1901 and SER D 180 source : AQ4 65) chain C residue 1644 type sequence F description binding site for Di-peptide PNS D 1901 and SER D 180 source : AQ4 66) chain C residue 1646 type sequence F description binding site for Di-peptide PNS D 1901 and SER D 180 source : AQ4 67) chain C residue 1305 type ACT_SITE sequence C description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 68) chain C residue 1542 type ACT_SITE sequence H description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 69) chain C residue 1583 type ACT_SITE sequence H description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 70) chain C residue 1772 type ACT_SITE sequence D description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 71) chain C residue 1773 type ACT_SITE sequence V description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 72) chain C residue 1774 type ACT_SITE sequence E description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 73) chain C residue 1817 type ACT_SITE sequence E description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 74) chain C residue 1841 type ACT_SITE sequence R description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 75) chain C residue 1871 type ACT_SITE sequence I description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 76) chain C residue 1872 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 77) chain C residue 1873 type ACT_SITE sequence H description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 78) chain C residue 1798 type MOD_RES sequence Y description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI3 79) chain C residue 1808 type MOD_RES sequence S description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI3 80) chain C residue 958 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 81) chain C residue 1440 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 82) chain C 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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