eF-site ID 5e8h-AB PDB Code 5e8h Chain A, B click to enlarge Title Crystal structure of geranylfarnesyl pyrophosphate synthases 2 from Arabidopsis thaliana Classification TRANSFERASE Compound Geranylgeranyl pyrophosphate synthase 3, chloroplastic Source (GGPP3_ARATH) Sequence A:  CNDHNSAFDFKLYMIRKAESVNAALDVSVPLREPLTVQEA VRYSLLAGGKRVRPLLCIAVCELVGGDEATAMSAACAVEM IHTSSLIHDDLPCMDNADLRRGKPTNHKVYGEDMAVLAGD ALLALAFEHMTVVSSGLVAPERMIRAVVELARAIGTTGLV AGQMIDLGLEHLEFIHLHKTAALLEAAAVLGVIMGGGTEE EIEKLRKYARCIGLLFQVVDDILDVTKSTEELTYPRLIGL ERSKEVAEKLRREAEEQLLGFDPSKAAPLVALASYIAC B:  HNSAFDFKLYMIRKAESVNAALDVSVPLREPVQEAVRYSL LAGGKRVRPLLCIAVCELVGGDEATAMSAACAVEMIHTSS LIHDDLPCMDNADLRRGKPTNHKVYGEDMAVLAGDALLAL AFEHMTVVSSGLVAPERMIRAVVELARAIGTTGLVAGQMI DLAVGLEHLEFIHLHKTAALLEAAAVLGVIMGGGTEEEIE KLRKYARCIGLLFQVVDDILDVLTYPRLIGLERSKEVAEK LRREAEEQLLGFDPSKAAPLVALASYIACR Description (1)  Geranylgeranyl pyrophosphate synthase 3, chloroplastic (E.C.2.5.1.-,2.5.1.1,2.5.1.29,2.5.1.10) Functional site 1) chain A residue 85 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:Q12051 source Swiss-Prot : SWS_FT_FI2 2) chain B residue 85 type BINDING sequence H description BINDING => ECO:0000250|UniProtKB:Q12051 source Swiss-Prot : SWS_FT_FI2 3) chain B residue 230 type BINDING sequence Q description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 4) chain A residue 193 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 5) chain A residue 230 type BINDING sequence Q description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 6) chain B residue 103 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 7) chain B residue 192 type BINDING sequence K description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 8) chain B residue 193 type BINDING sequence T description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 9) chain A residue 103 type BINDING sequence R description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 10) chain A residue 192 type BINDING sequence K description BINDING => ECO:0000250 source Swiss-Prot : SWS_FT_FI3 11) chain B residue 104 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P14324 source Swiss-Prot : SWS_FT_FI1 12) chain A residue 104 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P14324 source Swiss-Prot : SWS_FT_FI1 13) chain B residue 53 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P14324 source Swiss-Prot : SWS_FT_FI1 14) chain B residue 56 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P14324 source Swiss-Prot : SWS_FT_FI1 15) chain B residue 92 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P14324 source Swiss-Prot : SWS_FT_FI1 16) chain B residue 98 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P14324 source Swiss-Prot : SWS_FT_FI1 17) chain A residue 53 type BINDING sequence K description BINDING => ECO:0000250|UniProtKB:P14324 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 56 type BINDING sequence R description BINDING => ECO:0000250|UniProtKB:P14324 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 92 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P14324 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 98 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:P14324 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 225-237 type prosite sequence IGLLFQVVDDILD description POLYPRENYL_SYNTHASE_2 Polyprenyl synthases signature 2. IGllFQVvDDIlD source prosite : PS00444 22) chain A residue 89-105 type prosite sequence LIHDDLPCMDNADLRRG description POLYPRENYL_SYNTHASE_1 Polyprenyl synthases signature 1. LIhDDlpcmDnadlRRG source prosite : PS00723

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