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ModBase: Database of Comparative Protein Structure Models

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Sequence Information

Primary Database Link 46015526
Original Database ID GI 46015526
Organism Escherichia coli
Annotation b chain b, active conformation
of farnesyl pyrophosphate synthase
bound to isope ntyl pyrophosphate
and dimethylallyl s- thiolodiphosphate
Sequence Length 300

Dataset Information:

The newest dataset for this sequence was created on 2012-11-19. If you think that a better template has been added to the template database since, you can start a new calculation.

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Model Information

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Target Region2-300
Protein Length300
Template PDB Code1rqjA
Template Region22-320
Sequence Identity100%
E-Value0
GA3411
MPQS2.24987
z-DOPE-1.63
TSVMod MethodMTALL
TSVMod RMSD2.251
TSVMod NO350.965
Datasetefi_updates_1
ModPipe VersionSVN.r1372
Model Date2012-11-19

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Cross-references

Show obsolete/secondary identifiers
Template Structure
PDB1rqjactive conformation of farnesyl pyrophosphate synthase bound to isopentyl pyrophosphate and risedronate
DBALI1rqjA 
CATH1.10.600.10 Domain: 1rqjA00 Farnesyl Diphosphate Synthase (100%)
JenaImageLibrary1rqj 
Target Sequence
SFLD46015526Structure Function Linkage Database entry: Member of the Isoprenoid Synthase Type I superfamily.
PDB1RQIB Chain B, Active Conformation Of Farnesyl Pyrophosphate Synthase Bound To Isopentyl Pyrophosphate And Dimethylallyl S- Thiolodiphosphate
PDB1RQIAChain A, Active Conformation Of Farnesyl Pyrophosphate Synthase Bound To Isopentyl Pyrophosphate And Dimethylallyl S- Thiolodiphosphate
PDB1RQIBChain B, Active Conformation Of Farnesyl Pyrophosphate Synthase Bound To Isopentyl Pyrophosphate And Dimethylallyl S- Thiolodiphosphate
GenPept46015525A Chain A, Active Conformation Of Farnesyl Pyrophosphate Synthase Bound To Isopentyl Pyrophosphate And Dimethylallyl S- Thiolodiphosphate
GenPept46015526B Chain B, Active Conformation Of Farnesyl Pyrophosphate Synthase Bound To Isopentyl Pyrophosphate And Dimethylallyl S- Thiolodiphosphate