Structure of PDB 4lfv Chain F Binding Site BS05
Receptor Information
>4lfv Chain F (length=342) Species:
9606
(Homo sapiens) [
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DVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAIGGK
YNRGLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMD
SSLTRRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLI
ELFLQSSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFY
LPIAAAMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGK
IGTDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEE
LDLPAVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIY
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
4lfv Chain F Residue 405 [
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Receptor-Ligand Complex Structure
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PDB
4lfv
Structure of human farnesyl pyrophosphate synthase in complex with an aminopyridine bisphosphonate and two molecules of inorganic phosphate.
Resolution
2.0 Å
Binding residue
(original residue number in PDB)
D103 D107
Binding residue
(residue number reindexed from 1)
D96 D100
Annotation score
1
Enzymatic activity
Enzyme Commision number
2.5.1.1
: dimethylallyltranstransferase.
2.5.1.10
: (2E,6E)-farnesyl diphosphate synthase.
Gene Ontology
Molecular Function
GO:0004659
prenyltransferase activity
GO:0016765
transferase activity, transferring alkyl or aryl (other than methyl) groups
Biological Process
GO:0008299
isoprenoid biosynthetic process
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Molecular Function
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Biological Process
External links
PDB
RCSB:4lfv
,
PDBe:4lfv
,
PDBj:4lfv
PDBsum
4lfv
PubMed
24598914
UniProt
P14324
|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)
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