eF-site ID 2z78-AB PDB Code 2z78 Chain A, B click to enlarge Title S. cerevisiae geranylgeranyl pyrophosphate synthase in complex with BPH-806 Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound Geranylgeranyl pyrophosphate synthetase Source null (GGPPS_YEAST) Sequence A:  NKMEAKIDELINNDPVWSSQNESLISKPYNHILLKPGKNF RLNLIVQINRVMNLPKDQLAIVSQIVELLHNSSLLIDDIE DNAPLRRGQTTSHLIFGVPSTINTANYMYFRAMQLVSQLT TKEPLYHNLITIFNEELINLHRGQGLDIYWRDFLPEIIPT QEMYLNMVMNKTGGLFRLTLRLMEALSPSSHHGHSLVPFI NLLGIIYQIRDDYLNLKDFQMSKGFAEDITEGKLSFPIVH ALNFTKTKGQTEQHNEILRILLLRTSDKDIKLKLIQILEF DTNSLAYTKNFINQLVNMIKNDNENKYLPELLYIIDHLSE L B:  NKMEAKIDELINNDPVWSSQNESLISKPYNHILLKPGKNF RLNLIVQINRVMNLPKDQLAIVSQIVELLHNSSLLIDDIE DNAPLRRGQTTSHLIFGVPSTINTANYMYFRAMQLVSQLT TKEPLYHNLITIFNEELINLHRGQGLDIYWRDFLPEIIPT QEMYLNMVMNKTGGLFRLTLRLMEALSPSSHSLVPFINLL GIIYQIRDDYLNLKDFQMSGFAEDITEGKLSFPIVHALNF TKTKGQTEQHNEILRILLLRTSDKDIKLKLIQILEFDTNS LAYTKNFINQLVNMIKNDNENKYLPELLYIIDHLSEL Description Functional site 1) chain A residue 48 type sequence I description BINDING SITE FOR RESIDUE H86 A 1300 source : AC1 2) chain A residue 73 type sequence H description BINDING SITE FOR RESIDUE H86 A 1300 source : AC1 3) chain A residue 76 type sequence S description BINDING SITE FOR RESIDUE H86 A 1300 source : AC1 4) chain A residue 79 type sequence I description BINDING SITE FOR RESIDUE H86 A 1300 source : AC1 5) chain A residue 80 type sequence D description BINDING SITE FOR RESIDUE H86 A 1300 source : AC1 6) chain A residue 83 type sequence E description BINDING SITE FOR RESIDUE H86 A 1300 source : AC1 7) chain A residue 84 type sequence D description BINDING SITE FOR RESIDUE H86 A 1300 source : AC1 8) chain A residue 89 type sequence R description BINDING SITE FOR RESIDUE H86 A 1300 source : AC1 9) chain A residue 143 type sequence L description BINDING SITE FOR RESIDUE H86 A 1300 source : AC1 10) chain A residue 144 type sequence H description BINDING SITE FOR RESIDUE H86 A 1300 source : AC1 11) chain A residue 147 type sequence Q description BINDING SITE FOR RESIDUE H86 A 1300 source : AC1 12) chain A residue 175 type sequence T description BINDING SITE FOR RESIDUE H86 A 1300 source : AC1 13) chain A residue 179 type sequence F description BINDING SITE FOR RESIDUE H86 A 1300 source : AC1 14) chain A residue 210 type sequence Y description BINDING SITE FOR RESIDUE H86 A 1300 source : AC1 15) chain A residue 211 type sequence Q description BINDING SITE FOR RESIDUE H86 A 1300 source : AC1 16) chain A residue 214 type sequence D description BINDING SITE FOR RESIDUE H86 A 1300 source : AC1 17) chain A residue 238 type sequence K description BINDING SITE FOR RESIDUE H86 A 1300 source : AC1 18) chain A residue 340 type sequence L description BINDING SITE FOR RESIDUE H86 A 1300 source : AC1 19) chain B residue 47 type sequence L description BINDING SITE FOR RESIDUE H86 B 1301 source : AC2 20) chain B residue 73 type sequence H description BINDING SITE FOR RESIDUE H86 B 1301 source : AC2 21) chain B residue 76 type sequence S description BINDING SITE FOR RESIDUE H86 B 1301 source : AC2 22) chain B residue 77 type sequence L description BINDING SITE FOR RESIDUE H86 B 1301 source : AC2 23) chain B residue 80 type sequence D description BINDING SITE FOR RESIDUE H86 B 1301 source : AC2 24) chain B residue 89 type sequence R description BINDING SITE FOR RESIDUE H86 B 1301 source : AC2 25) chain B residue 143 type sequence L description BINDING SITE FOR RESIDUE H86 B 1301 source : AC2 26) chain B residue 147 type sequence Q description BINDING SITE FOR RESIDUE H86 B 1301 source : AC2 27) chain B residue 174 type sequence K description BINDING SITE FOR RESIDUE H86 B 1301 source : AC2 28) chain B residue 178 type sequence L description BINDING SITE FOR RESIDUE H86 B 1301 source : AC2 29) chain B residue 182 type sequence T description BINDING SITE FOR RESIDUE H86 B 1301 source : AC2 30) chain B residue 210 type sequence Y description BINDING SITE FOR RESIDUE H86 B 1301 source : AC2 31) chain B residue 211 type sequence Q description BINDING SITE FOR RESIDUE H86 B 1301 source : AC2 32) chain B residue 214 type sequence D description BINDING SITE FOR RESIDUE H86 B 1301 source : AC2 33) chain B residue 238 type sequence K description BINDING SITE FOR RESIDUE H86 B 1301 source : AC2 34) chain A residue 41 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 35) chain A residue 44 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 36) chain A residue 73 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 89 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 38) chain A residue 238 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 39) chain B residue 41 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 40) chain B residue 44 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 41) chain B residue 73 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 42) chain B residue 89 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 43) chain B residue 90 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 44) chain B residue 174 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 45) chain B residue 175 type BINDING sequence T description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 46) chain B residue 211 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 47) chain B residue 218 type BINDING sequence N description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 48) chain B residue 238 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 49) chain A residue 90 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 50) chain A residue 174 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 51) chain A residue 175 type BINDING sequence T description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 52) chain A residue 211 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 53) chain A residue 218 type BINDING sequence N description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 54) chain A residue 80 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16554305, ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI2 55) chain A residue 84 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16554305, ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI2 56) chain B residue 80 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16554305, ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI2 57) chain B residue 84 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16554305, ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI2 58) chain A residue 228 type BINDING sequence K description BINDING => ECO:0000305|PubMed:17535895 source Swiss-Prot : SWS_FT_FI3 59) chain A residue 112 type SITE sequence Y description Important for determining product chain length source Swiss-Prot : SWS_FT_FI4 60) chain B residue 112 type SITE sequence Y description Important for determining product chain length source Swiss-Prot : SWS_FT_FI4 61) chain A residue 206-218 type prosite sequence LGIIYQIRDDYLN description POLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. LGiiYQIrDDYlN source prosite : PS00444 62) chain A residue 77-91 type prosite sequence LLIDDIEDNAPLRRG description POLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LLiDDie..DnaplRRG source prosite : PS00723

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