eF-site ID 5ygi-A PDB Code 5ygi Chain A click to enlarge Title Crystal structure of human FPPS in complex with an inhibitor THZ93 Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound Farnesyl pyrophosphate synthase Source (FPPS_HUMAN) Sequence A:  DVYAQEKQDFVQHFSQIVRVLTEHPEIGDAIARLKEVLEY NAIGGKYNRGLTVVVAFRELVEPRKQDADSLQRAWTVGWC VELLQAFFLVADDIMDSSLTRRGQICWYQKPGVGLDAIND ANLLEACIYRLLKLYCREQPYYLNLIELFLQSSYQTEIGQ TLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPIA AAMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGD PSVTGKIGTDIQDNKCSWLVVQCLQRATPEQYQILKENYG QKEAEKVARVKALYEELDLPAVFLQYEEDSYSHIMALIEQ YAAPLPPAVFLGLARKIY Description Functional site 1) chain A residue 56 type sequence G description binding site for residue PO4 A 501 source : AC1 2) chain A residue 57 type sequence K description binding site for residue PO4 A 501 source : AC1 3) chain A residue 60 type sequence R description binding site for residue PO4 A 501 source : AC1 4) chain A residue 96 type sequence Q description binding site for residue PO4 A 501 source : AC1 5) chain A residue 113 type sequence R description binding site for residue PO4 A 501 source : AC1 6) chain A residue 60 type sequence R description binding site for residue PO4 A 502 source : AC2 7) chain A residue 96 type sequence Q description binding site for residue PO4 A 502 source : AC2 8) chain A residue 100 type sequence L description binding site for residue PO4 A 502 source : AC2 9) chain A residue 239 type sequence F description binding site for residue PO4 A 502 source : AC2 10) chain A residue 243 type sequence D description binding site for residue PO4 A 502 source : AC2 11) chain A residue 257 type sequence K description binding site for residue PO4 A 502 source : AC2 12) chain A residue 243 type sequence D description binding site for residue MG A 503 source : AC3 13) chain A residue 103 type sequence D description binding site for residue MG A 504 source : AC4 14) chain A residue 107 type sequence D description binding site for residue MG A 504 source : AC4 15) chain A residue 103 type sequence D description binding site for residue MG A 505 source : AC5 16) chain A residue 107 type sequence D description binding site for residue MG A 505 source : AC5 17) chain A residue 98 type sequence F description binding site for residue T93 A 506 source : AC6 18) chain A residue 99 type sequence F description binding site for residue T93 A 506 source : AC6 19) chain A residue 103 type sequence D description binding site for residue T93 A 506 source : AC6 20) chain A residue 106 type sequence M description binding site for residue T93 A 506 source : AC6 21) chain A residue 107 type sequence D description binding site for residue T93 A 506 source : AC6 22) chain A residue 112 type sequence R description binding site for residue T93 A 506 source : AC6 23) chain A residue 130 type sequence N description binding site for residue T93 A 506 source : AC6 24) chain A residue 133 type sequence N description binding site for residue T93 A 506 source : AC6 25) chain A residue 171 type sequence Q description binding site for residue T93 A 506 source : AC6 26) chain A residue 200 type sequence K description binding site for residue T93 A 506 source : AC6 27) chain A residue 201 type sequence T description binding site for residue T93 A 506 source : AC6 28) chain A residue 240 type sequence Q description binding site for residue T93 A 506 source : AC6 29) chain A residue 243 type sequence D description binding site for residue T93 A 506 source : AC6 30) chain A residue 257 type sequence K description binding site for residue T93 A 506 source : AC6 31) chain A residue 57 type BINDING sequence K description BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5 source Swiss-Prot : SWS_FT_FI1 32) chain A residue 60 type BINDING sequence R description BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5 source Swiss-Prot : SWS_FT_FI1 33) chain A residue 96 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5 source Swiss-Prot : SWS_FT_FI1 34) chain A residue 103 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 107 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 113 type BINDING sequence R description BINDING => ECO:0000269|PubMed:16684881, ECO:0007744|PDB:1ZW5 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 112 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 38) chain A residue 200 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 39) chain A residue 201 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 40) chain A residue 240 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI2 41) chain A residue 257 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 42) chain A residue 266 type BINDING sequence K description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 43) chain A residue 98 type SITE sequence F description Important for determining product chain length => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 44) chain A residue 99 type SITE sequence F description Important for determining product chain length => ECO:0000250 source Swiss-Prot : SWS_FT_FI4 45) chain A residue 57 type MOD_RES sequence K description N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5 46) chain A residue 287 type MOD_RES sequence K description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI6 47) chain A residue 235-247 type prosite sequence MGEFFQIQDDYLD description POLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. MGefFQIqDDYlD source prosite : PS00444 48) chain A residue 100-114 type prosite sequence LVADDIMDSSLTRRG description POLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LVaDDim..DssltRRG source prosite : PS00723

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