eF-site ID 6ql9-E PDB Code 6ql9 Chain E 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 E:  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 E residue 1251 type sequence M description binding site for residue EDO A 1910 source : AD1 2) chain E residue 1305 type sequence C description binding site for residue PNS B 1901 source : AE1 3) chain E residue 1346 type sequence M description binding site for residue PNS B 1901 source : AE1 4) chain E residue 1417 type sequence S description binding site for residue PNS B 1901 source : AE1 5) chain E residue 1419 type sequence P description binding site for residue PNS B 1901 source : AE1 6) chain E residue 1420 type sequence A description binding site for residue PNS B 1901 source : AE1 7) chain E residue 1542 type sequence H description binding site for residue PNS B 1901 source : AE1 8) chain E residue 1544 type sequence T description binding site for residue PNS B 1901 source : AE1 9) chain E residue 1546 type sequence T description binding site for residue PNS B 1901 source : AE1 10) chain E residue 1548 type sequence A description binding site for residue PNS B 1901 source : AE1 11) chain E residue 1549 type sequence N description binding site for residue PNS B 1901 source : AE1 12) chain E residue 1583 type sequence H description binding site for residue PNS B 1901 source : AE1 13) chain E residue 1644 type sequence F description binding site for residue PNS B 1901 source : AE1 14) chain E residue 1646 type sequence F description binding site for residue PNS B 1901 source : AE1 15) chain E residue 1428 type sequence T description binding site for residue EDO E 1902 source : AK3 16) chain E residue 1430 type sequence R description binding site for residue EDO E 1902 source : AK3 17) chain E residue 1635 type sequence G description binding site for residue EDO E 1903 source : AK4 18) chain E residue 1004 type sequence I description binding site for residue EDO E 1904 source : AK5 19) chain E residue 1636 type sequence V description binding site for residue EDO E 1904 source : AK5 20) chain E residue 1657 type sequence H description binding site for residue EDO E 1904 source : AK5 21) chain E residue 1110 type sequence L description binding site for residue EDO E 1905 source : AK6 22) chain E residue 1189 type sequence I description binding site for residue EDO E 1905 source : AK6 23) chain E residue 1380 type sequence Q description binding site for residue EDO E 1905 source : AK6 24) chain E residue 1183 type sequence R description binding site for residue EDO E 1906 source : AK7 25) chain E residue 1351 type sequence N description binding site for residue EDO E 1906 source : AK7 26) chain E residue 1354 type sequence E description binding site for residue EDO E 1906 source : AK7 27) chain E residue 1057 type sequence M description binding site for residue EDO E 1907 source : AK8 28) chain E residue 1059 type sequence F description binding site for residue EDO E 1907 source : AK8 29) chain E residue 1191 type sequence T description binding site for residue EDO E 1907 source : AK8 30) chain E residue 37 type sequence K description binding site for residue EDO E 1908 source : AK9 31) chain E residue 64 type sequence K description binding site for residue EDO E 1908 source : AK9 32) chain E residue 65 type sequence Y description binding site for residue EDO E 1908 source : AK9 33) chain E residue 935 type sequence E description binding site for residue EDO E 1909 source : AL1 34) chain E residue 335 type sequence H description binding site for residue EDO E 1910 source : AL2 35) chain E residue 342 type sequence Q description binding site for residue EDO E 1910 source : AL2 36) chain E residue 462 type sequence K description binding site for residue EDO E 1911 source : AL3 37) chain E residue 1634 type sequence D description binding site for residue EDO E 1911 source : AL3 38) chain E residue 1637 type sequence R description binding site for residue EDO E 1911 source : AL3 39) chain E residue 1601 type sequence N description binding site for residue EDO E 1912 source : AL4 40) chain E residue 1657 type sequence H description binding site for residue EDO E 1912 source : AL4 41) chain E residue 991 type sequence D description binding site for residue EDO E 1913 source : AL5 42) chain E residue 1037 type sequence W description binding site for residue EDO E 1913 source : AL5 43) chain E residue 1598 type sequence Q description binding site for residue EDO E 1913 source : AL5 44) chain E residue 1602 type sequence S description binding site for residue EDO E 1913 source : AL5 45) chain E residue 985 type sequence R description binding site for residue NA E 1914 source : AL6 46) chain E residue 1048 type sequence E description binding site for residue NA E 1914 source : AL6 47) chain E residue 1513 type sequence Y description binding site for residue NA E 1915 source : AL7 48) chain E residue 1514 type sequence K description binding site for residue NA E 1915 source : AL7 49) chain E residue 1516 type sequence D description binding site for residue NA E 1915 source : AL7 50) chain E residue 1519 type sequence I description binding site for residue NA E 1915 source : AL7 51) chain E residue 1098 type sequence L description binding site for residue NA E 1916 source : AL8 52) chain E residue 1101 type sequence S description binding site for residue NA E 1916 source : AL8 53) chain E residue 682 type sequence G description binding site for residue A2P E 1917 source : AL9 54) chain E residue 684 type sequence G description binding site for residue A2P E 1917 source : AL9 55) chain E residue 687 type sequence S description binding site for residue A2P E 1917 source : AL9 56) chain E residue 707 type sequence T description binding site for residue A2P E 1917 source : AL9 57) chain E residue 708 type sequence S description binding site for residue A2P E 1917 source : AL9 58) chain E residue 737 type sequence F description binding site for residue A2P E 1917 source : AL9 59) chain E residue 738 type sequence N description binding site for residue A2P E 1917 source : AL9 60) chain E residue 739 type sequence Q description binding site for residue A2P E 1917 source : AL9 61) chain E residue 772 type sequence A description binding site for residue A2P E 1917 source : AL9 62) chain E residue 773 type sequence A description binding site for residue A2P E 1917 source : AL9 63) chain E residue 774 type sequence I description binding site for residue A2P E 1917 source : AL9 64) chain E residue 352 type sequence M description binding site for residue PGE E 1918 source : AM1 65) chain E residue 178 type sequence G description binding site for Di-peptide PNS E 1901 and SER E 180 source : AQ5 66) chain E residue 179 type sequence K description binding site for Di-peptide PNS E 1901 and SER E 180 source : AQ5 67) chain E residue 181 type sequence T description binding site for Di-peptide PNS E 1901 and SER E 180 source : AQ5 68) chain E residue 182 type sequence V description binding site for Di-peptide PNS E 1901 and SER E 180 source : AQ5 69) chain E residue 183 type sequence Q description binding site for Di-peptide PNS E 1901 and SER E 180 source : AQ5 70) chain E residue 184 type sequence N description binding site for Di-peptide PNS E 1901 and SER E 180 source : AQ5 71) chain E residue 1305 type ACT_SITE sequence C description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 72) chain E residue 1542 type ACT_SITE sequence H description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 73) chain E residue 1583 type ACT_SITE sequence H description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 74) chain E residue 1772 type ACT_SITE sequence D description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 75) chain E residue 1773 type ACT_SITE sequence V description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 76) chain E residue 1774 type ACT_SITE sequence E description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 77) chain E residue 1817 type ACT_SITE sequence E description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 78) chain E residue 1841 type ACT_SITE sequence R description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 79) chain E residue 1871 type ACT_SITE sequence I description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 80) chain E residue 1872 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 81) chain E residue 1873 type ACT_SITE sequence H description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 82) chain E residue 1808 type MOD_RES sequence S description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI3 83) chain E residue 1798 type MOD_RES sequence Y description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI3 84) chain E residue 50 type MOD_RES sequence S description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI4 85) chain E residue 180 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI5 86) chain E residue 1440 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 87) chain E residue 958 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 88) chain E 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

Display surface Download Links