eF-site ID 3hmj-A PDB Code 3hmj Chain A click to enlarge Title Saccharomyces cerevisiae FAS type I Classification TRANSFERASE Compound Fatty acid synthase subunit alpha Source null (FAS1_YEAST) Sequence A:  MKPEVEQELAHILLTELLAYQFASPVRWIETQDVFLKDFN TERVVEIGPSPTLAGMAQRTLKNKYESYDAALSLHREILC YSKDAKEIYYTPDPIADEPVKASLLLHVLVAHKLKKSLDS IPMSKTIKDLVGGKSTVQNEILGDLGKEFGTTPEKPEETP LEELAETFQDTFSGALGKQSSSLLSRLISSKMPGGFTITV ARKYLQTRWGLPSGRQDGVLLVALSNEPAARLGSEADAKA FLDSMAQKYASIVGVDLLEEITKDHKVLARQQLQVLARYL KMDLDNGERKFLKEKDTVAELQAQLDYLNAELGEFFVNGV ATSFSRKKARTFDSSWNWAKQSLLSLYFEIIHGVLKNVDR EVVSEAINIMNRSNDALIKFMEYHISNTDETKGENYQLVK TLGEQLIENCKQVLDVDPVYKDVAKPTGPKTAIDKNGNIT YSEEPREKVRKLSQYVQEMALGGPITKESQMDVEDALDKD STKEVASLPNKSTISKTVSSTIPRETIPFLHLRKKTPAGD WKYDRQLSSLFLDGLEKAAFNGVTFKDKYVLITGAGKGSI GAEVLQGLLQGGAKVVVTTSRFSKQVTDYYQSIYAKYGAK GSTLIVVPFNQGSKQDVEALIEFIYDTEKNGGLGWDLDAI IPFAAIPEQGIELEHIDSKSEFAHRIMLTNILRMMGCVKK QKSARGIETRPAQVILPMSPNHGTFGGDGMYSESKLSLET LFNRWHSESWANQLTVCGAIIGWTRGTNNIIAEGIEKMGV RTFSQKEMAFNLLGLLTPEVVELCQKSPVMADLNGGLQFV PELKEFTAKLRKELVETSEVRKAVSIETALEHKVVNGNSA DAAYAQVEIQPRANIQLDFPELKPYKQVKQIAPAELEGLL DLERVIVVTGFAEVGPWGSARTRWEMEAFGEFSLEGCVEM AWIMGFISYHNGNLKGRPYTGWVDSKTKEPVDDKDVKAKY ETSILEHSGIRLIEPELFNGYNPEKKEMIQEVIVEEDLEP FEASKETAEQFKHQHGDKVDIFEIPETGEYSVKLLKGATL YIPKALRFDRLVAGQIPTGWNAKTYGISDDIISQVDPITL FVLVSVVEAFIASGITDPYEMYKYVHVSEVGNCSGSGMGG VSALRGMFKDRFKDEPVQNDILQESFINTMSAWVNMLLIS SSGPIKTPVGACATSVESVDIGVETILSGKARICIVGGYD DFQEEGSFEFGNMKATSNTLEEFEHGRTPAEMSRPATTTR NGFMEAQGAGIQIIMQADLALKMGVPIYGIVAMAATATDK IGRSVPAPGKGILTTAREHHSSVKYASPNLNMKYRKRQLV TREAQIKDWVENELEALKLEAEEIPSEDQNEFLLERTREI HNEAESQLRAAQQQWGNDFYKRDPRIAPLRGALATYGLTI DDLGVASFHGTSTKANDKNESATINEMMKHLGRSEGNPVI GVFQKFLTGHPKGAAGAWMMNGALQILNSGIIPGNRNADN VDKILEQFEYVLYPSKTLKTDGVRAVSITSFGFGQKGGQA IVVHPDYLYGAITEDRYNEYVAKVSAREKSAYKFFHNGMI YNKLFVSKEHAPYTDELEEDVYLDPLARVSKDKKSGSLTF NSKNIQSKDSYINTIETAKMIENMTKEKVSNGVGVDVELI TSINVENDTFIERNFTPQEIEYCSAQPSVQSSFAGTWSAK EAVFKSLGVKSLGGGAALKDIEIVRVNKNAPAVELHGNAK KAAEEAGVTDVKVSISHDDLQAVAVAVSTK Description Functional site 1) chain A residue 1279 type sequence F description BINDING SITE FOR RESIDUE CER A 2748 source : AC1 2) chain A residue 1304 type sequence A description BINDING SITE FOR RESIDUE CER A 2748 source : AC1 3) chain A residue 1305 type sequence C description BINDING SITE FOR RESIDUE CER A 2748 source : AC1 4) chain A residue 1343 type sequence F description BINDING SITE FOR RESIDUE CER A 2748 source : AC1 5) chain A residue 1542 type sequence H description BINDING SITE FOR RESIDUE CER A 2748 source : AC1 6) chain A residue 1583 type sequence H description BINDING SITE FOR RESIDUE CER A 2748 source : AC1 7) chain A residue 1585 type sequence K description BINDING SITE FOR RESIDUE CER A 2748 source : AC1 8) chain A residue 1644 type sequence F description BINDING SITE FOR RESIDUE CER A 2748 source : AC1 9) chain A residue 1646 type sequence F description BINDING SITE FOR RESIDUE CER A 2748 source : AC1 10) 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 11) chain A residue 1296-1312 type prosite sequence GPIKTPVGACATSVESV description KS3_1 Ketosynthase family 3 (KS3) active site signature. GPIktPVgACATSveSV source prosite : PS00606 12) chain A residue 1817 type ACT_SITE sequence E description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 13) chain A residue 1841 type ACT_SITE sequence R description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 14) chain A residue 1871 type ACT_SITE sequence I description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 1872 type ACT_SITE sequence S description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 16) chain A residue 1873 type ACT_SITE sequence H description For malonyltransferase activity => ECO:0000250 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 958 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 18) chain A residue 1440 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:17330950 source Swiss-Prot : SWS_FT_FI7 19) chain A residue 175-190 type prosite sequence LVGGKSTVQNEILGDL description PHOSPHOPANTETHEINE Phosphopantetheine attachment site. LVGGKSTVQNEILGDL source prosite : PS00012

Display surface Download Links