eF-site ID 2z4y-AB PDB Code 2z4y Chain A, B click to enlarge Title S. cerevisiae geranylgeranyl pyrophosphate synthase in complex with magnesium and BPH-252 Classification TRANSFERASE/TRANSFERASE INHIBITOR Compound Geranylgeranyl pyrophosphate synthetase Source Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) (GGPPS_YEAST) Sequence A:  NKMEAKIDELINNDPVWSSQNESLISKPYNHILLKPGRLN LIVQINRVMNLPKDQLAIVSQIVELLHNSSLLIDDIEDNA PLRRGQTTSHLIFGVPSTINTANYMYFRAMQLVSQLTTKE PLYHNLITIFNEELINLHRGQGLDIYWRDFLPEIIPTQEM YLNMVMNKTGGLFRLTLRLMEALSPSLVPFINLLGIIYQI RDDYLNLKDFQKGFAEDITEGKLSFPIVHALNFTKTKGQT EQHNEILRILLLRTSDKDIKLKLIQILEFDTNSLAYTKNF INQLVNMIKND B:  NKMEAKIDELINNDPVWSSQNESLISKPYNHILLIVQINR VMNLPKDQLAIVSQIVELLHNSSLLIDDIEDNAPLRRGQT TSHLIFGVPSTINTANYMYFRAMQLVSQLTTKEPLYHNLI TIFNEELINLHRGQGLDIYWRDFLPEIIPTQEMYLNMVMN KTGGLFRLTLRLMEALSPSSLVPFINLLGIIYQIRDDYLN LKDFGFAEDITEGKLSFPIVHALNFTKTKGQTEQHNEILR ILLLRTSDKDIKLKLIQILEFDTNSLAYTKNFINQLVNMI KN Description Functional site 1) chain B residue 214 type sequence D description BINDING SITE FOR RESIDUE MG B 1301 source : AC1 2) chain B residue 238 type sequence K description BINDING SITE FOR RESIDUE MG B 1301 source : AC1 3) chain A residue 80 type sequence D description BINDING SITE FOR RESIDUE 252 A 1201 source : AC2 4) chain A residue 89 type sequence R description BINDING SITE FOR RESIDUE 252 A 1201 source : AC2 5) chain A residue 174 type sequence K description BINDING SITE FOR RESIDUE 252 A 1201 source : AC2 6) chain A residue 211 type sequence Q description BINDING SITE FOR RESIDUE 252 A 1201 source : AC2 7) chain A residue 214 type sequence D description BINDING SITE FOR RESIDUE 252 A 1201 source : AC2 8) chain A residue 238 type sequence K description BINDING SITE FOR RESIDUE 252 A 1201 source : AC2 9) chain A residue 40 type sequence G description BINDING SITE FOR RESIDUE 252 A 1202 source : AC3 10) chain A residue 44 type sequence R description BINDING SITE FOR RESIDUE 252 A 1202 source : AC3 11) chain A residue 47 type sequence L description BINDING SITE FOR RESIDUE 252 A 1202 source : AC3 12) chain A residue 73 type sequence H description BINDING SITE FOR RESIDUE 252 A 1202 source : AC3 13) chain A residue 77 type sequence L description BINDING SITE FOR RESIDUE 252 A 1202 source : AC3 14) chain A residue 89 type sequence R description BINDING SITE FOR RESIDUE 252 A 1202 source : AC3 15) chain A residue 90 type sequence R description BINDING SITE FOR RESIDUE 252 A 1202 source : AC3 16) chain A residue 210 type sequence Y description BINDING SITE FOR RESIDUE 252 A 1202 source : AC3 17) chain B residue 80 type sequence D description BINDING SITE FOR RESIDUE 252 B 1203 source : AC4 18) chain B residue 89 type sequence R description BINDING SITE FOR RESIDUE 252 B 1203 source : AC4 19) chain B residue 143 type sequence L description BINDING SITE FOR RESIDUE 252 B 1203 source : AC4 20) chain B residue 144 type sequence H description BINDING SITE FOR RESIDUE 252 B 1203 source : AC4 21) chain B residue 174 type sequence K description BINDING SITE FOR RESIDUE 252 B 1203 source : AC4 22) chain B residue 211 type sequence Q description BINDING SITE FOR RESIDUE 252 B 1203 source : AC4 23) chain B residue 214 type sequence D description BINDING SITE FOR RESIDUE 252 B 1203 source : AC4 24) chain B residue 238 type sequence K description BINDING SITE FOR RESIDUE 252 B 1203 source : AC4 25) chain A residue 206-218 type prosite sequence LGIIYQIRDDYLN description POLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. LGiiYQIrDDYlN source prosite : PS00444 26) chain A residue 77-91 type prosite sequence LLIDDIEDNAPLRRG description POLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LLiDDie..DnaplRRG source prosite : PS00723 27) chain A residue 238 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 28) chain B residue 73 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 29) chain B residue 89 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 30) chain B residue 90 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 31) chain B residue 174 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 32) chain B residue 175 type BINDING sequence T description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 33) chain B residue 211 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 34) chain B residue 218 type BINDING sequence N 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 B residue 238 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 37) chain A residue 73 type BINDING sequence H description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 38) chain A residue 89 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 39) chain A residue 90 type BINDING sequence R description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 40) chain A residue 174 type BINDING sequence K description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 41) chain A residue 175 type BINDING sequence T description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 211 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 218 type BINDING sequence N description BINDING => ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI1 44) chain A residue 80 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16554305, ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI2 45) chain A residue 84 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16554305, ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI2 46) chain B residue 80 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16554305, ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI2 47) chain B residue 84 type BINDING sequence D description BINDING => ECO:0000269|PubMed:16554305, ECO:0000269|PubMed:17535895 source Swiss-Prot : SWS_FT_FI2 48) chain A residue 228 type BINDING sequence K description BINDING => ECO:0000305|PubMed:17535895 source Swiss-Prot : SWS_FT_FI3 49) chain A residue 112 type SITE sequence Y description Important for determining product chain length source Swiss-Prot : SWS_FT_FI4 50) chain B residue 112 type SITE sequence Y description Important for determining product chain length source Swiss-Prot : SWS_FT_FI4

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