Structure of PDB 2f92 Chain F Binding Site BS03
Receptor Information
>2f92 Chain F (length=343) Species:
9606
(Homo sapiens) [
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DVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAIGGK
YNRGLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMD
SSLTRRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLI
ELFLQSSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFY
LPIAAAMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGK
IGTDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEE
LDLPAVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYK
Ligand information
Ligand ID
PO4
InChI
InChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
InChIKey
NBIIXXVUZAFLBC-UHFFFAOYSA-K
SMILES
Software
SMILES
CACTVS 3.341
[O-][P]([O-])([O-])=O
ACDLabs 10.04
[O-]P([O-])([O-])=O
OpenEye OEToolkits 1.5.0
[O-]P(=O)([O-])[O-]
Formula
O4 P
Name
PHOSPHATE ION
ChEMBL
DrugBank
DB14523
ZINC
PDB chain
2f92 Chain F Residue 5001 [
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Receptor-Ligand Complex Structure
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PDB
2f92
Structural basis for the exceptional in vivo efficacy of bisphosphonate drugs.
Resolution
2.15 Å
Binding residue
(original residue number in PDB)
G56 R113
Binding residue
(residue number reindexed from 1)
G49 R106
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
View graph for
Molecular Function
View graph for
Biological Process
External links
PDB
RCSB:2f92
,
PDBe:2f92
,
PDBj:2f92
PDBsum
2f92
PubMed
16892359
UniProt
P14324
|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)
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