eF-site ID 1rqi-B PDB Code 1rqi Chain B click to enlarge Title Active Conformation of Farnesyl Pyrophosphate Synthase Bound to Isopentyl Pyrophosphate and Dimethylallyl S-Thiolodiphosphate Classification TRANSFERASE Compound Geranyltranstransferase Source (ISPA_ECOLI) Sequence B:  DFPQQLEACVKQANQALSRFIAPLPFQNTPVVETMQYGAL LGGKRLRPFLVYATGHMFGVSTNTLDAPAAAVECIHAYSL IHDDLPAMDDDDLRRGLPTCHVKFGEANAILAGDALQTLA FSILSDADMPEVSDRDRISMISELASASGIAGMCGGQALD LDAEGKHVPLDALERIHRHKTGALIRAAVRLGALSAGDKG RRALPVLDKYAESIGLAFQVQDDILDVVGDTATLGKRQGA DQQLGKSTYPALLGLEQARKKARDLIDDARQSLKQLAEQS LDTSALEALADYIIQRNK Description Functional site 1) chain B residue 244 type sequence D description BINDING SITE FOR RESIDUE MG B 600 source : AC1 2) chain B residue 248 type sequence D description BINDING SITE FOR RESIDUE MG B 600 source : AC1 3) chain B residue 105 type sequence D description BINDING SITE FOR RESIDUE MG B 601 source : AC2 4) chain B residue 111 type sequence D description BINDING SITE FOR RESIDUE MG B 601 source : AC2 5) chain B residue 105 type sequence D description BINDING SITE FOR RESIDUE MG B 602 source : AC3 6) chain B residue 111 type sequence D description BINDING SITE FOR RESIDUE MG B 602 source : AC3 7) chain B residue 101 type sequence S description BINDING SITE FOR RESIDUE DST B 400 source : AC7 8) chain B residue 105 type sequence D description BINDING SITE FOR RESIDUE DST B 400 source : AC7 9) chain B residue 111 type sequence D description BINDING SITE FOR RESIDUE DST B 400 source : AC7 10) chain B residue 116 type sequence R description BINDING SITE FOR RESIDUE DST B 400 source : AC7 11) chain B residue 175 type sequence M description BINDING SITE FOR RESIDUE DST B 400 source : AC7 12) chain B residue 179 type sequence Q description BINDING SITE FOR RESIDUE DST B 400 source : AC7 13) chain B residue 202 type sequence K description BINDING SITE FOR RESIDUE DST B 400 source : AC7 14) chain B residue 244 type sequence D description BINDING SITE FOR RESIDUE DST B 400 source : AC7 15) chain B residue 258 type sequence K description BINDING SITE FOR RESIDUE DST B 400 source : AC7 16) chain B residue 65 type sequence G description BINDING SITE FOR RESIDUE IPR B 500 source : AC9 17) chain B residue 66 type sequence K description BINDING SITE FOR RESIDUE IPR B 500 source : AC9 18) chain B residue 69 type sequence R description BINDING SITE FOR RESIDUE IPR B 500 source : AC9 19) chain B residue 98 type sequence H description BINDING SITE FOR RESIDUE IPR B 500 source : AC9 20) chain B residue 102 type sequence L description BINDING SITE FOR RESIDUE IPR B 500 source : AC9 21) chain B residue 117 type sequence R description BINDING SITE FOR RESIDUE IPR B 500 source : AC9 22) chain B residue 240 type sequence F description BINDING SITE FOR RESIDUE IPR B 500 source : AC9 23) chain B residue 241 type sequence Q description BINDING SITE FOR RESIDUE IPR B 500 source : AC9 24) chain B residue 244 type sequence D description BINDING SITE FOR RESIDUE IPR B 500 source : AC9 25) chain B residue 189 type sequence H description BINDING SITE FOR RESIDUE DPO A 606 source : BC2 26) chain B residue 105 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14672944 source Swiss-Prot : SWS_FT_FI1 27) chain B residue 111 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14672944 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 117 type BINDING sequence R description BINDING => ECO:0000269|PubMed:14672944 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 66 type BINDING sequence K description BINDING => ECO:0000269|PubMed:14672944 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 69 type BINDING sequence R description BINDING => ECO:0000269|PubMed:14672944 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 98 type BINDING sequence H description BINDING => ECO:0000269|PubMed:14672944 source Swiss-Prot : SWS_FT_FI1 32) chain B residue 258 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 33) chain B residue 116 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 34) chain B residue 202 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 35) chain B residue 203 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 36) chain B residue 241 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI2

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