Structure of PDB 2ewg Chain A Binding Site BS02
Receptor Information
>2ewg Chain A (length=367) Species:
5691
(Trypanosoma brucei) [
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MPMQMFMQVYDEIQMFLLEELELKFDMDPNRVRYLRKMMDTTCLGGKYNR
GLTVIDVAESLLSLSPNNNGEEDDGARRKRVLHDACVCGWMIEFLQAHYL
VEDDIMDNSVTRRGKPCWYRHPDVTVQCAINDGLLLKSWTHMMAMHFFAD
RPFLQDLLCRFNRVDYTTAVGQLYDVTSMFDSNKLDPDVSQPTTTDFAEF
TLSNYKRIVKYKTAYYTYLLPLVMGLIVSEALPTVDMGVTEELAMLMGEY
FQVQDDVMDCFTPPERLGKVGTDIQDAKCSWLAVTFLAKASSAQVAEFKA
NYGSGDSEKVATVRRLYEEADLQGDYVAYEAAVAEQVKELIEKLRLCSPG
FAASVETLWGKTYKRQK
Ligand information
Ligand ID
MG
InChI
InChI=1S/Mg/q+2
InChIKey
JLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
Software
SMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0
[Mg+2]
CACTVS 3.341
[Mg++]
Formula
Mg
Name
MAGNESIUM ION
ChEMBL
DrugBank
DB01378
ZINC
PDB chain
2ewg Chain A Residue 3003 [
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Receptor-Ligand Complex Structure
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PDB
2ewg
Solid-state NMR, crystallographic, and computational investigation of bisphosphonates and farnesyl diphosphate synthase-bisphosphonate complexes.
Resolution
2.48 Å
Binding residue
(original residue number in PDB)
D103 D107
Binding residue
(residue number reindexed from 1)
D103 D107
Annotation score
1
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
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Molecular Function
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Biological Process
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Cellular Component
External links
PDB
RCSB:2ewg
,
PDBe:2ewg
,
PDBj:2ewg
PDBsum
2ewg
PubMed
17090032
UniProt
Q86C09
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