eF-site ID 3o8o-H PDB Code 3o8o Chain H click to enlarge Title Structure of phosphofructokinase from Saccharomyces cerevisiae Classification TRANSFERASE Compound 6-phosphofructokinase subunit alpha Source (K6PF2_YEAST) Sequence H:  PQKAIAVMTSGGDAPGMNSNVRAIVRSAIFKGCRAFVVME GYEGLVRGGPEYIKEFHWEDVRGWSAEGGTNIGTARCMEF KKREGRLLGAQHLIEAGVDALIVCGGDGSLTGADLFRSEW PSLIEELLKTNRISNEQYERMKHLNICGTVGSIDNDMSTT DATIGAYSALDRICKAIDYVEATANSHSRAFVVEVMGRNC GWLALLAGIATSADYIFIPEKPATSSEWQDQMCDIVSKHR SRGKRTTIVVVAEGAIAADLTPISPSDVHKVLVDRLGLDT RITTLGHVQRGGTAVAYDRILATLQGLEAVNAVLESTPDT PSPLIAVNENKIVRKPLMESVKLTKAVAEAIQAKDFKRAM SLRDTEFIEHLNNFMAINSADHNEPKLPKDKRLKIAIVNV GAPAGGINSAVYSMATYCMSQGHRPYAIYNGWSGLARHES VRSLNWKDMLGWQSRGGSEIGTNRVTPEEADLGMIAYYFQ KYEFDGLIIVGGFEAFESLHQLERARESYPAFRIPMVLIP ATLSNNVPGTEYSLGSDTALNALMEYCDVVKQSASSTRGR AFVVDCQGGNSGYLATYASLAVGAQVSYVPEEGISLEQLS EDIEYLAQSFEKAEGRGRFGKLILKSTNASKALSATKLAE VITAEADGRFDAKPAYPGHVQQGGLPSPIDRTRATRMAIK AVGFIKDNQAAIAEARAAEENFNADDKTISDTAAVVGVKG SHVVYNSIRQLYDYETEVSMRMPKVIHWQATRLIADHLVG RKR Description Functional site 1) chain H residue 348 type ACT_SITE sequence D description Proton acceptor => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI1 2) chain H residue 206 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 3) chain H residue 270 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 4) chain H residue 300 type BINDING sequence G description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 5) chain H residue 301 type BINDING sequence D description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 6) chain H residue 754 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 7) chain H residue 847 type BINDING sequence K description BINDING => ECO:0000255|HAMAP-Rule:MF_03184 source Swiss-Prot : SWS_FT_FI2 8) chain H residue 346 type BINDING sequence S description BINDING => ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:21241708 source Swiss-Prot : SWS_FT_FI3 9) chain H residue 383 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:21241708 source Swiss-Prot : SWS_FT_FI3 10) chain H residue 390 type BINDING sequence M description BINDING => ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:21241708 source Swiss-Prot : SWS_FT_FI3 11) chain H residue 447 type BINDING sequence E description BINDING => ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:21241708 source Swiss-Prot : SWS_FT_FI3 12) chain H residue 475 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:21241708 source Swiss-Prot : SWS_FT_FI3 13) chain H residue 481 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:21241708 source Swiss-Prot : SWS_FT_FI3 14) chain H residue 658 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:21241708 source Swiss-Prot : SWS_FT_FI3 15) chain H residue 716 type BINDING sequence T description BINDING => ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:21241708 source Swiss-Prot : SWS_FT_FI3 16) chain H residue 761 type BINDING sequence Q description BINDING => ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:21241708 source Swiss-Prot : SWS_FT_FI3 17) chain H residue 853 type BINDING sequence H description BINDING => ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:21241708 source Swiss-Prot : SWS_FT_FI3 18) chain H residue 935 type BINDING sequence R description BINDING => ECO:0000255|HAMAP-Rule:MF_03184, ECO:0000269|PubMed:21241708 source Swiss-Prot : SWS_FT_FI3 19) chain H residue 803 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:18407956 source Swiss-Prot : SWS_FT_FI4

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