Structure of PDB 2ewg Chain A Binding Site BS03

Receptor Information
>2ewg Chain A (length=367) Species: 5691 (Trypanosoma brucei) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MPMQMFMQVYDEIQMFLLEELELKFDMDPNRVRYLRKMMDTTCLGGKYNR
GLTVIDVAESLLSLSPNNNGEEDDGARRKRVLHDACVCGWMIEFLQAHYL
VEDDIMDNSVTRRGKPCWYRHPDVTVQCAINDGLLLKSWTHMMAMHFFAD
RPFLQDLLCRFNRVDYTTAVGQLYDVTSMFDSNKLDPDVSQPTTTDFAEF
TLSNYKRIVKYKTAYYTYLLPLVMGLIVSEALPTVDMGVTEELAMLMGEY
FQVQDDVMDCFTPPERLGKVGTDIQDAKCSWLAVTFLAKASSAQVAEFKA
NYGSGDSEKVATVRRLYEEADLQGDYVAYEAAVAEQVKELIEKLRLCSPG
FAASVETLWGKTYKRQK
Ligand information
Ligand IDM0N
InChIInChI=1S/C9H12N2O7P2/c12-9(19(13,14)15,20(16,17)18)5-7-6-10-8-3-1-2-4-11(7)8/h1-4,6,12H,5H2,(H2,13,14,15)(H2,16,17,18)
InChIKeyVMMKGHQPQIEGSQ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04O=P(O)(O)C(O)(P(=O)(O)O)Cc1cnc2ccccn12
OpenEye OEToolkits 1.5.0c1ccn2c(c1)ncc2CC(O)(P(=O)(O)O)P(=O)(O)O
CACTVS 3.341OC(Cc1cnc2ccccn12)([P](O)(O)=O)[P](O)(O)=O
FormulaC9 H12 N2 O7 P2
Name(1-HYDROXY-2-IMIDAZO[1,2-A]PYRIDIN-3-YLETHANE-1,1-DIYL)BIS(PHOSPHONIC ACID);
MINODRONATE;
1-HYDROXY-2-(5,6,7,8-TETRAHYDROIMIDAZO[1,2-A]PYRIDIN-3-YL)ETHANE-1,1-DIYLDIPHOSPONIC ACID;
(1-HYDROXY-2-IMIDAZO[1,2-A]PYRIDIN-3-YL-ETHYLIDENE)-1,1-BISPHOSPHONIC ACID
ChEMBLCHEMBL319144
DrugBankDB06548
ZINCZINC000003803518
PDB chain2ewg Chain A Residue 3001 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2ewg Solid-state NMR, crystallographic, and computational investigation of bisphosphonates and farnesyl diphosphate synthase-bisphosphonate complexes.
Resolution2.48 Å
Binding residue
(original residue number in PDB)
Y99 D103 D107 R112 T168 Q172 K212 T213 Y216
Binding residue
(residue number reindexed from 1)
Y99 D103 D107 R112 T168 Q172 K212 T213 Y216
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) K47 H98 D103 D107 R112 D175 K212 F251 D255 D256
Catalytic site (residue number reindexed from 1) K47 H98 D103 D107 R112 D175 K212 F251 D255 D256
Enzyme Commision number 2.5.1.10: (2E,6E)-farnesyl diphosphate synthase.
Gene Ontology
Molecular Function
GO:0004161 dimethylallyltranstransferase activity
GO:0004337 geranyltranstransferase activity
GO:0004659 prenyltransferase activity
GO:0016740 transferase activity
GO:0016765 transferase activity, transferring alkyl or aryl (other than methyl) groups
GO:0046872 metal ion binding
Biological Process
GO:0008299 isoprenoid biosynthetic process
GO:0045337 farnesyl diphosphate biosynthetic process
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:2ewg, PDBe:2ewg, PDBj:2ewg
PDBsum2ewg
PubMed17090032
UniProtQ86C09

[Back to BioLiP]