eF-site ID 3n1v-F PDB Code 3n1v Chain F click to enlarge Title Human FPPS COMPLEX WITH FBS_01 Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound FARNESYL PYROPHOSPHATE SYNTHASE Source null (FPPS_HUMAN) Sequence F:  DVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKE VLEYNAIGGKYNRGLTVVVAFRELVEPRKQDADSLQRAWT VGWCVELLQAFFLVADDIMDSSLTRRGQICWYQKPGVGLD AINDANLLEACIYRLLKLYCREQPYYLNLIELFLQSSYQT EIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFY LPIAAAMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLD LFGDPSVTGKIGTDIQDNKCSWLVVQCLQRATPEQYQILK ENYGQKEAEKVARVKALYEELDLPAVFLQYEEDSYSHIMA LIEQYAAPLPPAVFLGLARKIYK Description Functional site 1) chain F residue 10 type sequence Y description BINDING SITE FOR RESIDUE 3N1 F 1 source : AC1 2) chain F residue 57 type sequence K description BINDING SITE FOR RESIDUE 3N1 F 1 source : AC1 3) chain F residue 59 type sequence N description BINDING SITE FOR RESIDUE 3N1 F 1 source : AC1 4) chain F residue 60 type sequence R description BINDING SITE FOR RESIDUE 3N1 F 1 source : AC1 5) chain F residue 63 type sequence T description BINDING SITE FOR RESIDUE 3N1 F 1 source : AC1 6) chain F residue 205 type sequence S description BINDING SITE FOR RESIDUE 3N1 F 1 source : AC1 7) chain F residue 206 type sequence F description BINDING SITE FOR RESIDUE 3N1 F 1 source : AC1 8) chain F residue 239 type sequence F description BINDING SITE FOR RESIDUE 3N1 F 1 source : AC1 9) chain F residue 344 type sequence L description BINDING SITE FOR RESIDUE 3N1 F 1 source : AC1 10) chain F residue 347 type sequence K description BINDING SITE FOR RESIDUE 3N1 F 1 source : AC1 11) chain F residue 114 type sequence G description BINDING SITE FOR RESIDUE 3N1 F 354 source : AC2 12) chain F residue 315 type sequence L description BINDING SITE FOR RESIDUE 3N1 F 354 source : AC2 13) chain F residue 318 type sequence E description BINDING SITE FOR RESIDUE 3N1 F 354 source : AC2 14) chain F residue 322 type sequence Y description BINDING SITE FOR RESIDUE 3N1 F 354 source : AC2 15) chain F residue 56 type sequence G description BINDING SITE FOR RESIDUE PO4 F 355 source : AC3 16) chain F residue 57 type sequence K description BINDING SITE FOR RESIDUE PO4 F 355 source : AC3 17) chain F residue 96 type sequence Q description BINDING SITE FOR RESIDUE PO4 F 355 source : AC3 18) chain F residue 113 type sequence R description BINDING SITE FOR RESIDUE PO4 F 355 source : AC3 19) chain F residue 235-247 type prosite sequence MGEFFQIQDDYLD description POLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. MGefFQIqDDYlD source prosite : PS00444 20) chain F residue 287 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 21) chain F residue 57 type BINDING sequence K description BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5 source Swiss-Prot : SWS_FT_FI1 22) chain F residue 60 type BINDING sequence R description BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5 source Swiss-Prot : SWS_FT_FI1 23) chain F residue 96 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5 source Swiss-Prot : SWS_FT_FI1 24) chain F residue 103 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5 source Swiss-Prot : SWS_FT_FI1 25) chain F residue 107 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5 source Swiss-Prot : SWS_FT_FI1 26) chain F residue 113 type BINDING sequence R description BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5 source Swiss-Prot : SWS_FT_FI1 27) chain F residue 112 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 28) chain F residue 200 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 29) chain F residue 201 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 30) chain F residue 257 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 31) chain F residue 240 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI2 32) chain F residue 266 type BINDING sequence K description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 33) chain F residue 98 type SITE sequence F description Important for determining product chain length => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 34) chain F residue 99 type SITE sequence F description Important for determining product chain length => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 35) chain F residue 57 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5 36) chain F residue 100-114 type prosite sequence LVADDIMDSSLTRRG description POLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LVaDDim..DssltRRG source prosite : PS00723

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