eF-site ID 6ql5-D PDB Code 6ql5 Chain D click to enlarge Title Structure of fatty acid synthase complex with bound gamma subunit from Saccharomyces cerevisiae at 2.8 angstrom Classification TRANSFERASE Compound Fatty acid synthase subunit alpha Source ORGANISM_COMMON: Baker's yeast; ORGANISM_SCIENTIFIC: Saccharomyces cerevisiae; Sequence D:  MKPEVEQELAHILLTELLAYQFASPVRWIETQDVFLKDFN TERVVEIGPSPTLAGMAQRTLKNKYESYDAALSLHREILC YSKDAKEIYYTPDPIADEPVKASLLLHVLVAHKLKKSLDS IPMSKTIKDLVGGKSTVQNEILGDLGKEFGTTPEKPEETP LEELAETFQDTFSGALGKQSSSLLSRLISSKMPGGFTITV ARKYLQTRWGLPSGRQDGVLLVALSNEPAARLGSEADAKA FLDSMAQKYASIVGVDLLEEITKDHKVLARQQLQVLARYL KMDLDNGERKFLKEKDTVAELQAQLDYLNAELGEFFVNGV ATSFSRKKARTFDSSWNWAKQSLLSLYFEIIHGVLKNVDR EVVSEAINIMNRSNDALIKFMEYHISNTDETKGENYQLVK TLGEQLIENCKQVLDVDPVYKDVAKPTGPKTAIDKNGNIT YSEEPREKVRKLSQYVQEMALGGPITKESALDKDSTKEVA SLPNKSTISKTVSSTIPRETIPFLHLRKKTPAGDWKYDRQ LSSLFLDGLEKAAFNGVTFKDKYVLITGAGKGSIGAEVLQ GLLQGGAKVVVTTSRFSKQVTDYYQSIYAKYGAKGSTLIV VPFNQGSKQDVEALIEFIYDTEKNGGLGWDLDAIIPFAAI PEQGIELEHIDSKSEFAHRIMLTNILRMMGCVKKQKSARG IETRPAQVILPMSPNHGTFGGDGMYSESKLSLETLFNRWH SESWANQLTVCGAIIGWTRGTGLMSANNIIAEGIEKMGVR TFSQKEMAFNLLGLLTPEVVELCQKSPVMADLNGGLQFVP ELKEFTAKLRKELVETSEVRKAVSIETALEHKVVNGNSAD AAYAQVEIQPRANIQLDFPELKPYKQVKQIAPAELEGLLD LERVIVVTGFAEVGPWGSARTRWEMEAFGEFSLEGCVEMA WIMGFISYHNGNLKGRPYTGWVDSKTKEPVDDKDVKAKYE TSILEHSGIRLIEPELFNGYNPEKKEMIQEVIVEEDLEPF EASKETAEQFKHQHGDKVDIFEIPETGEYSVKLLKGATLY IPKALRFDRLVAGQIPTGWNAKTYGISDDIISQVDPITLF VLVSVVEAFIASGITDPYEMYKYVHVSEVGNCSGSGMGGV SALRGMFKDRFKDEPVQNDILQESFINTMSAWVNMLLISS SGPIKTPVGACATSVESVDIGVETILSGKARICIVGGYDD FQEEGSFEFGNMKATSNTLEEFEHGRTPAEMSRPATTTRN GFMEAQGAGIQIIMQADLALKMGVPIYGIVAMAATATDKI GRSVPAPGKGILTTAREHHSSVKYASPNLNMKYRKRQLVT REAQIKDWVENELEALKLEAEEIPSEDQNEFLLERTREIH NEAESQLRAAQQQWGNDFYKRDPRIAPLRGALATYGLTID DLGVASFHGTSTKANDKNESATINEMMKHLGRSEGNPVIG VFQKFLTGHPKGAAGAWMMNGALQILNSGIIPGNRNADNV DKILEQFEYVLYPSKTLKTDGVRAVSITSFGFGQKGGQAI VVHPDYLYGAITEDRYNEYVAKVSAREKSAYKFFHNGMIY NKLFVSKEHAPYTDELEEDVYLDPLARVSKDKKSGSLTFN SKNIQSKDSYINANTIETAKMIENMTKEKVSNGGVGVDVE LITSINVENDTFIERNFTPQEIEYCSAQPSVQSSFAGTWS AKEAVFKSLGVKSLGGGAALKDIEIVRVNKNAPAVELHGN AKKAAEEAGVTDVKVSISHDDLQAVAVAVSTK Description (1)  Fatty acid synthase subunit alpha (E.C.2.3.1.86,1.1.1.100,2.3.1.41), Fatty acid synthase subunit beta (E.C.2.3.1.86,4.2.1.59,1.3.1.9,2.3.1.38,2.3.1.39,3.1.2.14), Translation machinery-associated protein 17 Functional site 1) chain D residue 178 type sequence G description binding site for Di-peptide PNS D 1901 and SER D 180 source : AD1 2) chain D residue 179 type sequence K description binding site for Di-peptide PNS D 1901 and SER D 180 source : AD1 3) chain D residue 181 type sequence T description binding site for Di-peptide PNS D 1901 and SER D 180 source : AD1 4) chain D residue 182 type sequence V description binding site for Di-peptide PNS D 1901 and SER D 180 source : AD1 5) chain D residue 183 type sequence Q description binding site for Di-peptide PNS D 1901 and SER D 180 source : AD1 6) chain D residue 184 type sequence N description binding site for Di-peptide PNS D 1901 and SER D 180 source : AD1 7) chain D residue 1305 type MOD_RES sequence C description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 8) chain D residue 1542 type MOD_RES sequence H description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 9) chain D residue 1583 type MOD_RES sequence H description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI1 10) chain D residue 1772 type MOD_RES sequence D description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI2 11) chain D residue 1773 type MOD_RES sequence V description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI2 12) chain D residue 1774 type MOD_RES sequence E description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI2 13) chain D residue 1817 type MOD_RES sequence E description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI2 14) chain D residue 1841 type MOD_RES sequence R description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI2 15) chain D residue 1871 type MOD_RES sequence I description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI2 16) chain D residue 1872 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI2 17) chain D residue 1873 type MOD_RES sequence H description Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI2 18) chain D residue 1798 type MOD_RES sequence Y description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI3 19) chain D residue 1808 type MOD_RES sequence S description Phosphothreonine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI3 20) chain D residue 180 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_FI5 21) chain D residue 523 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 22) chain D residue 958 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 23) chain D residue 1440 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 24) 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

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