eF-site ID 6ql9-D PDB Code 6ql9 Chain D 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 D:  MKPEVEQELAHILLTELLAYQFASPVRWIETQDVFLKDFN TERVVEIGPSPTLAGMAQRTLKNKYESYDAALSLHREILC YSKDAKEIYYTPDPSEIADEPVKASLLLHVLVAHKLKKSL DSIPMSKTIKDLVGGKSTVQNEILGDLGKEFGTTPEKPEE TPLEELAETFQDTFSGALGKQSSSLLSRLISSKMPGGFTI TVARKYLQTRWGLPSGRQDGVLLVALSNEPAARLGSEADA KAFLDSMAQKYASIVGVDLLEEITKDHKVLARQQLQVLAR YLKMDLDNGERKFLKEKDTVAELQAQLDYLNAELGEFFVN GVATSFSRKKARTFDSSWNWAKQSLLSLYFEIIHGVLKNV DREVVSEAINIMNRSNDALIKFMEYHISNTDETKGENYQL VKTLGEQLIENCKQVLDVDPVYKDVAKPTGPKTAIDKNGN ITYSEEPREKVRKLSQYVQEMALGGPITKESQPTIEEMDV EDALDKDSTKEVASLPNKSTISKTVSSTIPRETIPFLHLR KKTPAGDWKYDRQLSSLFLDGLEKAAFNGVTFKDKYVLIT GAGKGSIGAEVLQGLLQGGAKVVVTTSRFSKQVTDYYQSI YAKYGAKGSTLIVVPFNQGSKQDVEALIEFIYDTEKNGGL GWDLDAIIPFAAIPEQGIELEHIDSKSEFAHRIMLTNILR MMGCVKKQKSARGIETRPAQVILPMSPNHGTFGGDGMYSE SKLSLETLFNRWHSESWANQLTVCGAIIGWTRGTGLMSAN NIIAEGIEKMGVRTFSQKEMAFNLLGLLTPEVVELCQKSP VMADLNGGLQFVPELKEFTAKLRKELVETSEVRKAVSIET ALEHKVVNGNSADAAYAQVEIQPRANIQLDFPELKPYKQV KQIAPAELEGLLDLERVIVVTGFAEVGPWGSARTRWEMEA FGEFSLEGCVEMAWIMGFISYHNGNLKGRPYTGWVDSKTK EPVDDKDVKAKYETSILEHSGIRLIEPELFNGYNPEKKEM IQEVIVEEDLEPFEASKETAEQFKHQHGDKVDIFEIPETG EYSVKLLKGATLYIPKALRFDRLVAGQIPTGWNAKTYGIS DDIISQVDPITLFVLVSVVEAFIASGITDPYEMYKYVHVS EVGNCSGSGMGGVSALRGMFKDRFKDEPVQNDILQESFIN TMSAWVNMLLISSSGPIKTPVGACATSVESVDIGVETILS GKARICIVGGYDDFQEEGSFEFGNMKATSNTLEEFEHGRT PAEMSRPATTTRNGFMEAQGAGIQIIMQADLALKMGVPIY GIVAMAATATDKIGRSVPAPGKGILTTAREHHSSVKYASP NLNMKYRKRQLVTREAQIKDWVENELEALKLEAEEIPSED QNEFLLERTREIHNEAESQLRAAQQQWGNDFYKRDPRIAP LRGALATYGLTIDDLGVASFHGTSTKANDKNESATINEMM KHLGRSEGNPVIGVFQKFLTGHPKGAAGAWMMNGALQILN SGIIPGNRNADNVDKILEQFEYVLYPSKTLKTDGVRAVSI TSFGFGQKGGQAIVVHPDYLYGAITEDRYNEYVAKVSARE KSAYKFFHNGMIYNKLFVSKEHAPYTDELEEDVYLDPLAR VSKDKKSGSLTFNSKNIQSKDSYINANTIETAKMIENMTK EKVSNGGVGVDVELITSINVENDTFIERNFTPQEIEYCSA QPSVQSSFAGTWSAKEAVFKSLGVKSLGGGAALKDIEIVR VNKNAPAVELHGNAKKAAEEAGVTDVKVSISHDDLQAVAV AVSTK Description Functional site 1) chain D residue 1251 type sequence M description binding site for residue EDO B 1911 source : AF1 2) chain D residue 1278 type sequence S description binding site for residue EDO B 1911 source : AF1 3) chain D residue 1305 type sequence C description binding site for residue PNS C 1901 source : AF9 4) chain D residue 1346 type sequence M description binding site for residue PNS C 1901 source : AF9 5) chain D residue 1417 type sequence S description binding site for residue PNS C 1901 source : AF9 6) chain D residue 1419 type sequence P description binding site for residue PNS C 1901 source : AF9 7) chain D residue 1420 type sequence A description binding site for residue PNS C 1901 source : AF9 8) chain D residue 1542 type sequence H description binding site for residue PNS C 1901 source : AF9 9) chain D residue 1544 type sequence T description binding site for residue PNS C 1901 source : AF9 10) chain D residue 1546 type sequence T description binding site for residue PNS C 1901 source : AF9 11) chain D residue 1548 type sequence A description binding site for residue PNS C 1901 source : AF9 12) chain D residue 1549 type sequence N description binding site for residue PNS C 1901 source : AF9 13) chain D residue 1583 type sequence H description binding site for residue PNS C 1901 source : AF9 14) chain D residue 1644 type sequence F description binding site for residue PNS C 1901 source : AF9 15) chain D residue 1646 type sequence F description binding site for residue PNS C 1901 source : AF9 16) chain D residue 828 type sequence P description binding site for residue EDO C 1909 source : AG8 17) chain D residue 830 type sequence H description binding site for residue EDO C 1909 source : AG8 18) chain D residue 397 type sequence K description binding site for residue EDO D 1902 source : AH8 19) chain D residue 1358 type sequence H description binding site for residue EDO D 1902 source : AH8 20) chain D residue 1372 type sequence T description binding site for residue EDO D 1902 source : AH8 21) chain D residue 398 type sequence K description binding site for residue EDO D 1903 source : AH9 22) chain D residue 1145 type sequence K description binding site for residue EDO D 1904 source : AI1 23) chain D residue 1153 type sequence D description binding site for residue EDO D 1904 source : AI1 24) chain D residue 1154 type sequence I description binding site for residue EDO D 1904 source : AI1 25) chain D residue 1004 type sequence I description binding site for residue EDO D 1905 source : AI2 26) chain D residue 1635 type sequence G description binding site for residue EDO D 1905 source : AI2 27) chain D residue 1657 type sequence H description binding site for residue EDO D 1905 source : AI2 28) chain D residue 1194 type sequence N description binding site for residue EDO D 1906 source : AI3 29) chain D residue 1195 type sequence A description binding site for residue EDO D 1906 source : AI3 30) chain D residue 1110 type sequence L description binding site for residue EDO D 1907 source : AI4 31) chain D residue 1189 type sequence I description binding site for residue EDO D 1907 source : AI4 32) chain D residue 1190 type sequence P description binding site for residue EDO D 1907 source : AI4 33) chain D residue 1380 type sequence Q description binding site for residue EDO D 1907 source : AI4 34) chain D residue 454 type sequence H description binding site for residue EDO D 1908 source : AI5 35) chain D residue 1635 type sequence G description binding site for residue EDO D 1908 source : AI5 36) chain D residue 417 type sequence Y description binding site for residue EDO D 1909 source : AI6 37) chain D residue 454 type sequence H description binding site for residue EDO D 1909 source : AI6 38) chain D residue 492 type sequence D description binding site for residue EDO D 1910 source : AI7 39) chain D residue 691 type sequence E description binding site for residue EDO D 1910 source : AI7 40) chain D residue 694 type sequence Q description binding site for residue EDO D 1910 source : AI7 41) chain D residue 698 type sequence Q description binding site for residue EDO D 1910 source : AI7 42) chain D residue 899 type sequence K description binding site for residue EDO D 1910 source : AI7 43) chain D residue 1057 type sequence M description binding site for residue EDO D 1911 source : AI8 44) chain D residue 1191 type sequence T description binding site for residue EDO D 1911 source : AI8 45) chain D residue 1197 type sequence T description binding site for residue EDO D 1912 source : AI9 46) chain D residue 935 type sequence E description binding site for residue EDO D 1913 source : AJ1 47) chain D residue 1228 type sequence I description binding site for residue EDO D 1914 source : AJ2 48) chain D residue 1229 type sequence T description binding site for residue EDO D 1914 source : AJ2 49) chain D residue 1697 type sequence L description binding site for residue EDO D 1914 source : AJ2 50) chain D residue 985 type sequence R description binding site for residue NA D 1915 source : AJ3 51) chain D residue 1048 type sequence E description binding site for residue NA D 1915 source : AJ3 52) chain D residue 1206 type sequence S description binding site for residue NA D 1916 source : AJ4 53) chain D residue 1208 type sequence V description binding site for residue NA D 1916 source : AJ4 54) chain D residue 1271 type sequence Q description binding site for residue NA D 1916 source : AJ4 55) chain D residue 400 type sequence R description binding site for residue NA D 1917 source : AJ5 56) chain D residue 715 type sequence T description binding site for residue NA D 1917 source : AJ5 57) chain D residue 1360 type sequence R description binding site for residue NA D 1917 source : AJ5 58) chain D residue 1612 type sequence D description binding site for residue NA D 1917 source : AJ5 59) chain D residue 1026 type sequence E description binding site for residue NA D 1918 source : AJ6 60) chain D residue 1028 type sequence G description binding site for residue NA D 1918 source : AJ6 61) chain D residue 1036 type sequence R description binding site for residue NA D 1918 source : AJ6 62) chain D residue 1209 type sequence D description binding site for residue NA D 1919 source : AJ7 63) chain D residue 1212 type sequence T description binding site for residue NA D 1919 source : AJ7 64) chain D residue 1277 type sequence E description binding site for residue NA D 1919 source : AJ7 65) chain D residue 1283 type sequence M description binding site for residue NA D 1919 source : AJ7 66) chain D residue 1340 type sequence S description binding site for residue NA D 1920 source : AJ8 67) chain D residue 1378 type sequence E description binding site for residue NA D 1920 source : AJ8 68) chain D residue 716 type sequence D description binding site for residue NA D 1921 source : AJ9 69) chain D residue 719 type sequence Q description binding site for residue NA D 1921 source : AJ9 70) chain D residue 1609 type sequence R description binding site for residue NA D 1921 source : AJ9 71) chain D residue 1106 type sequence I description binding site for residue NA D 1922 source : AK1 72) chain D residue 1114 type sequence Y description binding site for residue NA D 1922 source : AK1 73) chain D residue 1181 type sequence F description binding site for residue NA D 1922 source : AK1 74) chain D residue 1183 type sequence R description binding site for residue NA D 1922 source : AK1 75) chain D residue 1340 type sequence S description binding site for residue NA D 1922 source : AK1 76) chain D residue 682 type sequence G description binding site for residue A2P D 1923 source : AK2 77) chain D residue 684 type sequence G description binding site for residue A2P D 1923 source : AK2 78) chain D residue 707 type sequence T description binding site for residue A2P D 1923 source : AK2 79) chain D residue 708 type sequence S description binding site for residue A2P D 1923 source : AK2 80) chain D residue 709 type sequence R description binding site for residue A2P D 1923 source : AK2 81) chain D residue 738 type sequence N description binding site for residue A2P D 1923 source : AK2 82) chain D residue 739 type sequence Q description binding site for residue A2P D 1923 source : AK2 83) chain D residue 772 type sequence A description binding site for residue A2P D 1923 source : AK2 84) chain D residue 773 type sequence A description binding site for residue A2P D 1923 source : AK2 85) chain D residue 774 type sequence I description binding site for residue A2P D 1923 source : AK2 86) chain D residue 335 type sequence H description binding site for residue EDO E 1910 source : AL2 87) chain D residue 342 type sequence Q description binding site for residue EDO E 1910 source : AL2 88) chain D residue 178 type sequence G description binding site for Di-peptide PNS D 1901 and SER D 180 source : AQ4 89) chain D residue 179 type sequence K description binding site for Di-peptide PNS D 1901 and SER D 180 source : AQ4 90) chain D residue 181 type sequence T description binding site for Di-peptide PNS D 1901 and SER D 180 source : AQ4 91) chain D residue 182 type sequence V description binding site for Di-peptide PNS D 1901 and SER D 180 source : AQ4 92) chain D residue 183 type sequence Q description binding site for Di-peptide PNS D 1901 and SER D 180 source : AQ4 93) chain D residue 184 type sequence N description binding site for Di-peptide PNS D 1901 and SER D 180 source : AQ4 94) chain D residue 958 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 95) chain D residue 1440 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 96) chain D residue 1305 type ACT_SITE sequence C description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 97) chain D residue 1542 type ACT_SITE sequence H description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 98) chain D residue 1583 type ACT_SITE sequence H description For acetyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI1 99) chain D residue 1772 type ACT_SITE sequence D description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 100) chain D residue 1773 type ACT_SITE sequence V description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 101) chain D residue 1774 type ACT_SITE sequence E description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 102) chain D residue 1817 type ACT_SITE sequence E description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 103) chain D residue 1841 type ACT_SITE sequence R description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 104) chain D residue 1871 type ACT_SITE sequence I description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 105) chain D residue 1872 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 106) chain D residue 1873 type ACT_SITE sequence H description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 107) chain D residue 1798 type MOD_RES sequence Y description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI3 108) chain D residue 1808 type MOD_RES sequence S description N-acetylmethionine => ECO:0007744|PubMed:22814378 source Swiss-Prot : SWS_FT_FI3 109) chain D 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 110) chain D 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