eF-site ID 6ql6-B PDB Code 6ql6 Chain B 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; Sequence B:  MKPEVEQELAHILLTELLAYQFASPVRWIETQDVFLKDFN TERVVEIGPSPTLAGMAQRTLKNKYESYDAALSLHREILC YSKDAKEIYYTPDPIADEPVKASLLLHVLVAHKLKKSLDS IPMSKTIKDLVGGKSTVQNEILGDLGKEFGTTPEKPEETP LEELAETFQDTFSGALGKQSSSLLSRLISSKMPGGFTITV ARKYLQTRWGLPSGRQDGVLLVALSNEPAARLGSEADAKA FLDSMAQKYASIVGVDLLEEITKDHKVLARQQLQVLARYL KMDLDNGERKFLKEKDTVAELQAQLDYLNAELGEFFVNGV ATSFSRKKARTFDSSWNWAKQSLLSLYFEIIHGVLKNVDR EVVSEAINIMNRSNDALIKFMEYHISNTDETKGENYQLVK TLGEQLIENCKQVLDVDPVYKDVAKPTGPKTAIDKNGNIT YSEEPREKVRKLSQYVQEMALGGPITKESMDVEDALDKDS TKEVASLPNKSTISKTVSSTIPRETIPFLHLRKKTPAGDW KYDRQLSSLFLDGLEKAAFNGVTFKDKYVLITGAGKGSIG AEVLQGLLQGGAKVVVTTSRFSKQVTDYYQSIYAKYGAKG STLIVVPFNQGSKQDVEALIEFIYDTEKNGGLGWDLDAII PFAAIPEQGIELEHIDSKSEFAHRIMLTNILRMMGCVKKQ KSARGIETRPAQVILPMSPNHGTFGGDGMYSESKLSLETL FNRWHSESWANQLTVCGAIIGWTRGTGLMSANNIIAEGIE KMGVRTFSQKEMAFNLLGLLTPEVVELCQKSPVMADLNGG LQFVPELKEFTAKLRKELVETSEVRKAVSIETALEHKVVN GNSADAAYAQVEIQPRANIQLDFPELKPYKQVKQIAPAEL EGLLDLERVIVVTGFAEVGPWGSARTRWEMEAFGEFSLEG CVEMAWIMGFISYHNGNLKGRPYTGWVDSKTKEPVDDKDV KAKYETSILEHSGIRLIEPELFNGYNPEKKEMIQEVIVEE DLEPFEASKETAEQFKHQHGDKVDIFEIPETGEYSVKLLK GATLYIPKALRFDRLVAGQIPTGWNAKTYGISDDIISQVD PITLFVLVSVVEAFIASGITDPYEMYKYVHVSEVGNCSGS GMGGVSALRGMFKDRFKDEPVQNDILQESFINTMSAWVNM LLISSSGPIKTPVGACATSVESVDIGVETILSGKARICIV GGYDDFQEEGSFEFGNMKATSNTLEEFEHGRTPAEMSRPA TTTRNGFMEAQGAGIQIIMQADLALKMGVPIYGIVAMAAT ATDKIGRSVPAPGKGILTTAREHHSSVKYASPNLNMKYRK RQLVTREAQIKDWVENELEALKLEAEEIPSEDQNEFLLER TREIHNEAESQLRAAQQQWGNDFYKRDPRIAPLRGALATY GLTIDDLGVASFHGTSTKANDKNESATINEMMKHLGRSEG NPVIGVFQKFLTGHPKGAAGAWMMNGALQILNSGIIPGNR NADNVDKILEQFEYVLYPSKTLKTDGVRAVSITSFGFGQK GGQAIVVHPDYLYGAITEDRYNEYVAKVSAREKSAYKFFH NGMIYNKLFVSKEHAPYTDELEEDVYLDPLARVSKDKKSG SLTFNSKNIQSKDSYINANTIETAKMIENMTKEKVSNGGV GVDVELITSINVENDTFIERNFTPQEIEYCSAQPSVQSSF AGTWSAKEAVFKSLGVKSLGGGAALKDIEIVRVNKNAPAV ELHGNAKKAAEEAGVTDVKVSISHDDLQAVAVAVSTK 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) Functional site 1) chain B residue 178 type sequence G description binding site for Di-peptide J8T B 1901 and SER B 180 source : AC8 2) chain B residue 179 type sequence K description binding site for Di-peptide J8T B 1901 and SER B 180 source : AC8 3) chain B residue 181 type sequence T description binding site for Di-peptide J8T B 1901 and SER B 180 source : AC8 4) chain B residue 182 type sequence V description binding site for Di-peptide J8T B 1901 and SER B 180 source : AC8 5) chain B residue 183 type sequence Q description binding site for Di-peptide J8T B 1901 and SER B 180 source : AC8 6) chain B residue 184 type sequence N description binding site for Di-peptide J8T B 1901 and SER B 180 source : AC8 7) chain B residue 1417 type sequence S description binding site for Di-peptide J8T E 1901 and SER E 180 source : AD2 8) chain B residue 1419 type sequence P description binding site for Di-peptide J8T E 1901 and SER E 180 source : AD2 9) chain B residue 1420 type sequence A description binding site for Di-peptide J8T E 1901 and SER E 180 source : AD2 10) chain B residue 1548 type sequence A description binding site for Di-peptide J8T E 1901 and SER E 180 source : AD2 11) chain B 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 12) chain B residue 1772 type ACT_SITE sequence D description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 13) chain B residue 1773 type ACT_SITE sequence V description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 14) chain B residue 1774 type ACT_SITE sequence E description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 15) chain B residue 1817 type ACT_SITE sequence E description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 16) chain B residue 1841 type ACT_SITE sequence R description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 17) chain B residue 1871 type ACT_SITE sequence I description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 18) chain B residue 1872 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 19) chain B residue 1873 type ACT_SITE sequence H description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 20) chain B 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 B residue 523 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:19779198 source Swiss-Prot : SWS_FT_FI6 22) chain B residue 958 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 23) chain B residue 1440 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7

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