eF-site ID 1rqi-AB PDB Code 1rqi Chain A, 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 A:  AMDFPQQLEACVKQANQALSRFIAPLPFQNTPVVETMQYG ALLGGKRLRPFLVYATGHMFGVSTNTLDAPAAAVECIHAY SLIHDDLPAMDDDDLRRGLPTCHVKFGEANAILAGDALQT LAFSILSDADMPEVSDRDRISMISELASASGIAGMCGGQA LDLDAEGKHVPLDALERIHRHKTGALIRAAVRLGALSAGD KGRRALPVLDKYAESIGLAFQVQDDILDVVGDTATLGKRQ GADQQLGKSTYPALLGLEQARKKARDLIDDARQSLKQLAE QSLDTSALEALADYIIQRNK 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 A residue 244 type sequence D description BINDING SITE FOR RESIDUE MG A 603 source : AC4 8) chain A residue 105 type sequence D description BINDING SITE FOR RESIDUE MG A 604 source : AC5 9) chain A residue 111 type sequence D description BINDING SITE FOR RESIDUE MG A 604 source : AC5 10) chain A residue 105 type sequence D description BINDING SITE FOR RESIDUE MG A 605 source : AC6 11) chain A residue 111 type sequence D description BINDING SITE FOR RESIDUE MG A 605 source : AC6 12) chain A residue 113 type sequence D description BINDING SITE FOR RESIDUE MG A 605 source : AC6 13) chain B residue 101 type sequence S description BINDING SITE FOR RESIDUE DST B 400 source : AC7 14) chain B residue 105 type sequence D description BINDING SITE FOR RESIDUE DST B 400 source : AC7 15) chain B residue 111 type sequence D description BINDING SITE FOR RESIDUE DST B 400 source : AC7 16) chain B residue 116 type sequence R description BINDING SITE FOR RESIDUE DST B 400 source : AC7 17) chain B residue 175 type sequence M description BINDING SITE FOR RESIDUE DST B 400 source : AC7 18) chain B residue 179 type sequence Q description BINDING SITE FOR RESIDUE DST B 400 source : AC7 19) chain B residue 202 type sequence K description BINDING SITE FOR RESIDUE DST B 400 source : AC7 20) chain B residue 244 type sequence D description BINDING SITE FOR RESIDUE DST B 400 source : AC7 21) chain B residue 258 type sequence K description BINDING SITE FOR RESIDUE DST B 400 source : AC7 22) chain A residue 101 type sequence S description BINDING SITE FOR RESIDUE DST A 401 source : AC8 23) chain A residue 102 type sequence L description BINDING SITE FOR RESIDUE DST A 401 source : AC8 24) chain A residue 105 type sequence D description BINDING SITE FOR RESIDUE DST A 401 source : AC8 25) chain A residue 111 type sequence D description BINDING SITE FOR RESIDUE DST A 401 source : AC8 26) chain A residue 116 type sequence R description BINDING SITE FOR RESIDUE DST A 401 source : AC8 27) chain A residue 175 type sequence M description BINDING SITE FOR RESIDUE DST A 401 source : AC8 28) chain A residue 179 type sequence Q description BINDING SITE FOR RESIDUE DST A 401 source : AC8 29) chain A residue 202 type sequence K description BINDING SITE FOR RESIDUE DST A 401 source : AC8 30) chain A residue 244 type sequence D description BINDING SITE FOR RESIDUE DST A 401 source : AC8 31) chain A residue 258 type sequence K description BINDING SITE FOR RESIDUE DST A 401 source : AC8 32) chain B residue 65 type sequence G description BINDING SITE FOR RESIDUE IPR B 500 source : AC9 33) chain B residue 66 type sequence K description BINDING SITE FOR RESIDUE IPR B 500 source : AC9 34) chain B residue 69 type sequence R description BINDING SITE FOR RESIDUE IPR B 500 source : AC9 35) chain B residue 98 type sequence H description BINDING SITE FOR RESIDUE IPR B 500 source : AC9 36) chain B residue 102 type sequence L description BINDING SITE FOR RESIDUE IPR B 500 source : AC9 37) chain B residue 117 type sequence R description BINDING SITE FOR RESIDUE IPR B 500 source : AC9 38) chain B residue 240 type sequence F description BINDING SITE FOR RESIDUE IPR B 500 source : AC9 39) chain B residue 241 type sequence Q description BINDING SITE FOR RESIDUE IPR B 500 source : AC9 40) chain B residue 244 type sequence D description BINDING SITE FOR RESIDUE IPR B 500 source : AC9 41) chain A residue 65 type sequence G description BINDING SITE FOR RESIDUE IPR A 501 source : BC1 42) chain A residue 66 type sequence K description BINDING SITE FOR RESIDUE IPR A 501 source : BC1 43) chain A residue 69 type sequence R description BINDING SITE FOR RESIDUE IPR A 501 source : BC1 44) chain A residue 98 type sequence H description BINDING SITE FOR RESIDUE IPR A 501 source : BC1 45) chain A residue 117 type sequence R description BINDING SITE FOR RESIDUE IPR A 501 source : BC1 46) chain A residue 203 type sequence T description BINDING SITE FOR RESIDUE IPR A 501 source : BC1 47) chain A residue 240 type sequence F description BINDING SITE FOR RESIDUE IPR A 501 source : BC1 48) chain A residue 241 type sequence Q description BINDING SITE FOR RESIDUE IPR A 501 source : BC1 49) chain A residue 244 type sequence D description BINDING SITE FOR RESIDUE IPR A 501 source : BC1 50) chain A residue 27 type sequence Q description BINDING SITE FOR RESIDUE DPO A 606 source : BC2 51) chain A residue 30 type sequence A description BINDING SITE FOR RESIDUE DPO A 606 source : BC2 52) chain A residue 31 type sequence C description BINDING SITE FOR RESIDUE DPO A 606 source : BC2 53) chain A residue 34 type sequence Q description BINDING SITE FOR RESIDUE DPO A 606 source : BC2 54) chain A residue 71 type sequence F description BINDING SITE FOR RESIDUE DPO A 606 source : BC2 55) chain A residue 74 type sequence Y description BINDING SITE FOR RESIDUE DPO A 606 source : BC2 56) chain A residue 75 type sequence A description BINDING SITE FOR RESIDUE DPO A 606 source : BC2 57) chain A residue 78 type sequence H description BINDING SITE FOR RESIDUE DPO A 606 source : BC2 58) chain B residue 189 type sequence H description BINDING SITE FOR RESIDUE DPO A 606 source : BC2 59) chain A residue 66 type BINDING sequence K description BINDING => ECO:0000269|PubMed:14672944 source Swiss-Prot : SWS_FT_FI1 60) chain A residue 69 type BINDING sequence R description BINDING => ECO:0000269|PubMed:14672944 source Swiss-Prot : SWS_FT_FI1 61) chain A residue 98 type BINDING sequence H description BINDING => ECO:0000269|PubMed:14672944 source Swiss-Prot : SWS_FT_FI1 62) chain A residue 105 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14672944 source Swiss-Prot : SWS_FT_FI1 63) chain B residue 105 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14672944 source Swiss-Prot : SWS_FT_FI1 64) chain B residue 111 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14672944 source Swiss-Prot : SWS_FT_FI1 65) chain B residue 117 type BINDING sequence R description BINDING => ECO:0000269|PubMed:14672944 source Swiss-Prot : SWS_FT_FI1 66) chain A residue 111 type BINDING sequence D description BINDING => ECO:0000269|PubMed:14672944 source Swiss-Prot : SWS_FT_FI1 67) chain A residue 117 type BINDING sequence R description BINDING => ECO:0000269|PubMed:14672944 source Swiss-Prot : SWS_FT_FI1 68) chain B residue 66 type BINDING sequence K description BINDING => ECO:0000269|PubMed:14672944 source Swiss-Prot : SWS_FT_FI1 69) chain B residue 69 type BINDING sequence R description BINDING => ECO:0000269|PubMed:14672944 source Swiss-Prot : SWS_FT_FI1 70) chain B residue 98 type BINDING sequence H description BINDING => ECO:0000269|PubMed:14672944 source Swiss-Prot : SWS_FT_FI1 71) chain A residue 116 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 72) chain A residue 202 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 73) chain A residue 203 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 74) chain A residue 241 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI2 75) chain A residue 258 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 76) chain B residue 116 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI2 77) chain B residue 202 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 78) chain B residue 203 type BINDING sequence T description source Swiss-Prot : SWS_FT_FI2 79) chain B residue 258 type BINDING sequence K description source Swiss-Prot : SWS_FT_FI2 80) chain B residue 241 type BINDING sequence Q description source Swiss-Prot : SWS_FT_FI2 81) chain A residue 236-248 type prosite sequence IGLAFQVQDDILD description POLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. IGlaFQVqDDIlD source prosite : PS00444 82) chain A residue 102-118 type prosite sequence LIHDDLPAMDDDDLRRG description POLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LIhDDlpamDdddlRRG source prosite : PS00723

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