eF-site ID 6ql9-A PDB Code 6ql9 Chain A 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 A:  MKPEVEQELAHILLTELLAYQFASPVRWIETQDVFLKDFN TERVVEIGPSPTLAGMAQRTLKNKYESYDAALSLHREILC YSKDAKEIYYTPDPSEIADEPVKASLLLHVLVAHKLKKSL DSIPMSKTIKDLVGGKSTVQNEILGDLGKEFGTTPEKPEE TPLEELAETFQDTFSGALGKQSSSLLSRLISSKMPGGFTI TVARKYLQTRWGLPSGRQDGVLLVALSNEPAARLGSEADA KAFLDSMAQKYASIVGVDLSLEEITKDHKVLARQQLQVLA RYLKMDLDNGERKFLKEKDTVAELQAQLDYLNAELGEFFV NGVATSFSRKKARTFDSSWNWAKQSLLSLYFEIIHGVLKN VDREVVSEAINIMNRSNDALIKFMEYHISNTDETKGENYQ LVKTLGEQLIENCKQVLDVDPVYKDVAKPTGPKTAIDKNG NITYSEEPREKVRKLSQYVQEMALGGPITKESMDVEDALD KDSTKEVASLPNKSTISKTVSSTIPRETIPFLHLRKKTPA GDWKYDRQLSSLFLDGLEKAAFNGVTFKDKYVLITGAGKG SIGAEVLQGLLQGGAKVVVTTSRFSKQVTDYYQSIYAKYG AKGSTLIVVPFNQGSKQDVEALIEFIYDTEKNGGLGWDLD AIIPFAAIPEQGIELEHIDSKSEFAHRIMLTNILRMMGCV KKQKSARGIETRPAQVILPMSPNHGTFGGDGMYSESKLSL ETLFNRWHSESWANQLTVCGAIIGWTRGTGLMSANNIIAE GIEKMGVRTFSQKEMAFNLLGLLTPEVVELCQKSPVMADL NGGLQFVPELKEFTAKLRKELVETSEVRKAVSIETALEHK VVNGNSADAAYAQVEIQPRANIQLDFPELKPYKQVKQIAP AELEGLLDLERVIVVTGFAEVGPWGSARTRWEMEAFGEFS LEGCVEMAWIMGFISYHNGNLKGRPYTGWVDSKTKEPVDD KDVKAKYETSILEHSGIRLIEPELFNGYNPEKKEMIQEVI VEEDLEPFEASKETAEQFKHQHGDKVDIFEIPETGEYSVK LLKGATLYIPKALRFDRLVAGQIPTGWNAKTYGISDDIIS QVDPITLFVLVSVVEAFIASGITDPYEMYKYVHVSEVGNC SGSGMGGVSALRGMFKDRFKDEPVQNDILQESFINTMSAW VNMLLISSSGPIKTPVGACATSVESVDIGVETILSGKARI CIVGGYDDFQEEGSFEFGNMKATSNTLEEFEHGRTPAEMS RPATTTRNGFMEAQGAGIQIIMQADLALKMGVPIYGIVAM AATATDKIGRSVPAPGKGILTTAREHHSSVKYASPNLNMK YRKRQLVTREAQIKDWVENELEALKLEAEEIPSEDQNEFL LERTREIHNEAESQLRAAQQQWGNDFYKRDPRIAPLRGAL ATYGLTIDDLGVASFHGTSTKANDKNESATINEMMKHLGR SEGNPVIGVFQKFLTGHPKGAAGAWMMNGALQILNSGIIP GNRNADNVDKILEQFEYVLYPSKTLKTDGVRAVSITSFGF GQKGGQAIVVHPDYLYGAITEDRYNEYVAKVSAREKSAYK FFHNGMIYNKLFVSKEHAPYTDELEEDVYLDPLARVSKDK KSGSLTFNSKNIQSKDSYINANTIETAKMIENMTKEKVSN GGVGVDVELITSINVENDTFIERNFTPQEIEYCSAQPSVQ SSFAGTWSAKEAVFKSLGVKSLGGGAALKDIEIVRVNKNA PAVELHGNAKKAAEEAGVTDVKVSISHDDLQAVAVAVSTK Description Functional site 1) chain A residue 180 type sequence S description binding site for residue PNS A 1901 source : AC1 2) chain A residue 184 type sequence N description binding site for residue PNS A 1901 source : AC1 3) chain A residue 1110 type sequence L description binding site for residue EDO A 1902 source : AC2 4) chain A residue 1111 type sequence F description binding site for residue EDO A 1902 source : AC2 5) chain A residue 1380 type sequence Q description binding site for residue EDO A 1902 source : AC2 6) chain A residue 398 type sequence K description binding site for residue EDO A 1903 source : AC3 7) chain A residue 1223 type sequence F description binding site for residue EDO A 1904 source : AC4 8) chain A residue 1228 type sequence I description binding site for residue EDO A 1904 source : AC4 9) chain A residue 1229 type sequence T description binding site for residue EDO A 1904 source : AC4 10) chain A residue 1231 type sequence P description binding site for residue EDO A 1904 source : AC4 11) chain A residue 1697 type sequence L description binding site for residue EDO A 1904 source : AC4 12) chain A residue 1057 type sequence M description binding site for residue EDO A 1905 source : AC5 13) chain A residue 1059 type sequence F description binding site for residue EDO A 1905 source : AC5 14) chain A residue 1635 type sequence G description binding site for residue EDO A 1906 source : AC6 15) chain A residue 1636 type sequence V description binding site for residue EDO A 1906 source : AC6 16) chain A residue 1657 type sequence H description binding site for residue EDO A 1906 source : AC6 17) chain A residue 492 type sequence D description binding site for residue EDO A 1907 source : AC7 18) chain A residue 691 type sequence E description binding site for residue EDO A 1907 source : AC7 19) chain A residue 694 type sequence Q description binding site for residue EDO A 1907 source : AC7 20) chain A residue 698 type sequence Q description binding site for residue EDO A 1907 source : AC7 21) chain A residue 935 type sequence E description binding site for residue EDO A 1908 source : AC8 22) chain A residue 1194 type sequence N description binding site for residue EDO A 1909 source : AC9 23) chain A residue 1195 type sequence A description binding site for residue EDO A 1909 source : AC9 24) chain A residue 1213 type sequence L description binding site for residue EDO A 1909 source : AC9 25) chain A residue 1251 type sequence M description binding site for residue EDO A 1910 source : AD1 26) chain A residue 1278 type sequence S description binding site for residue EDO A 1910 source : AD1 27) chain A residue 335 type sequence H description binding site for residue EDO A 1911 source : AD2 28) chain A residue 342 type sequence Q description binding site for residue EDO A 1911 source : AD2 29) chain A residue 985 type sequence R description binding site for residue NA A 1912 source : AD3 30) chain A residue 1048 type sequence E description binding site for residue NA A 1912 source : AD3 31) chain A residue 1106 type sequence I description binding site for residue NA A 1913 source : AD4 32) chain A residue 1114 type sequence Y description binding site for residue NA A 1913 source : AD4 33) chain A residue 1181 type sequence F description binding site for residue NA A 1913 source : AD4 34) chain A residue 1183 type sequence R description binding site for residue NA A 1913 source : AD4 35) chain A residue 1340 type sequence S description binding site for residue NA A 1913 source : AD4 36) chain A residue 1034 type sequence R description binding site for residue NA A 1914 source : AD5 37) chain A residue 1052 type sequence E description binding site for residue NA A 1914 source : AD5 38) chain A residue 1198 type sequence Y description binding site for residue NA A 1914 source : AD5 39) chain A residue 1221 type sequence E description binding site for residue NA A 1914 source : AD5 40) chain A residue 1206 type sequence S description binding site for residue NA A 1915 source : AD6 41) chain A residue 1271 type sequence Q description binding site for residue NA A 1915 source : AD6 42) chain A residue 1209 type sequence D description binding site for residue NA A 1916 source : AD7 43) chain A residue 1212 type sequence T description binding site for residue NA A 1916 source : AD7 44) chain A residue 1277 type sequence E description binding site for residue NA A 1916 source : AD7 45) chain A residue 1283 type sequence M description binding site for residue NA A 1916 source : AD7 46) chain A residue 1209 type sequence D description binding site for residue NA A 1917 source : AD8 47) chain A residue 1254 type sequence V description binding site for residue NA A 1917 source : AD8 48) chain A residue 1255 type sequence S description binding site for residue NA A 1917 source : AD8 49) chain A residue 1334 type sequence D description binding site for residue NA A 1917 source : AD8 50) chain A residue 682 type sequence G description binding site for residue A2P A 1918 source : AD9 51) chain A residue 684 type sequence G description binding site for residue A2P A 1918 source : AD9 52) chain A residue 687 type sequence S description binding site for residue A2P A 1918 source : AD9 53) chain A residue 707 type sequence T description binding site for residue A2P A 1918 source : AD9 54) chain A residue 708 type sequence S description binding site for residue A2P A 1918 source : AD9 55) chain A residue 709 type sequence R description binding site for residue A2P A 1918 source : AD9 56) chain A residue 737 type sequence F description binding site for residue A2P A 1918 source : AD9 57) chain A residue 738 type sequence N description binding site for residue A2P A 1918 source : AD9 58) chain A residue 739 type sequence Q description binding site for residue A2P A 1918 source : AD9 59) chain A residue 772 type sequence A description binding site for residue A2P A 1918 source : AD9 60) chain A residue 773 type sequence A description binding site for residue A2P A 1918 source : AD9 61) chain A residue 774 type sequence I description binding site for residue A2P A 1918 source : AD9 62) chain A residue 1323 type sequence K description binding site for residue EDO E 1902 source : AK3 63) chain A residue 1346 type sequence M description binding site for Di-peptide PNS F 1901 and SER F 180 source : AQ6 64) chain A residue 1417 type sequence S description binding site for Di-peptide PNS F 1901 and SER F 180 source : AQ6 65) chain A residue 1419 type sequence P description binding site for Di-peptide PNS F 1901 and SER F 180 source : AQ6 66) chain A residue 1420 type sequence A description binding site for Di-peptide PNS F 1901 and SER F 180 source : AQ6 67) chain A residue 1544 type sequence T description binding site for Di-peptide PNS F 1901 and SER F 180 source : AQ6 68) chain A residue 1546 type sequence T description binding site for Di-peptide PNS F 1901 and SER F 180 source : AQ6 69) chain A residue 1548 type sequence A description binding site for Di-peptide PNS F 1901 and SER F 180 source : AQ6 70) chain A residue 1549 type sequence N description binding site for Di-peptide PNS F 1901 and SER F 180 source : AQ6 71) chain A residue 1644 type sequence F description binding site for Di-peptide PNS F 1901 and SER F 180 source : AQ6 72) chain A residue 175-190 type prosite sequence LVGGKSTVQNEILGDL description PHOSPHOPANTETHEINE Phosphopantetheine attachment site. LVGGKSTVQNEILGDL source prosite : PS00012 73) chain A residue 1296-1312 type prosite sequence GPIKTPVGACATSVESV description KS3_1 Ketosynthase family 3 (KS3) active site signature. GPIktPVgACATSveSV source prosite : PS00606 74) chain A residue 1841 type ACT_SITE sequence R description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 75) chain A residue 1871 type ACT_SITE sequence I description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 76) chain A residue 1872 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 77) chain A residue 1873 type ACT_SITE sequence H description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 78) chain A residue 958 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 79) chain A residue 1440 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 80) chain A 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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