Structure of PDB 4n9u Chain A Binding Site BS03

Receptor Information
>4n9u Chain A (length=338) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DVYAQEKQDFVQHFSQIVRVLTEHPEIGDAIARLKEVLEYNTIGGKYNRG
LTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLT
RRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFL
QSSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYGTAFYSFYLPIA
AAMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTD
IQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLP
AVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIY
Ligand information
Ligand IDRIS
InChIInChI=1S/C7H11NO7P2/c9-7(16(10,11)12,17(13,14)15)4-6-2-1-3-8-5-6/h1-3,5,9H,4H2,(H2,10,11,12)(H2,13,14,15)
InChIKeyIIDJRNMFWXDHID-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341OC(Cc1cccnc1)([P](O)(O)=O)[P](O)(O)=O
ACDLabs 10.04O=P(O)(O)C(O)(P(=O)(O)O)Cc1cccnc1
OpenEye OEToolkits 1.5.0c1cc(cnc1)CC(O)(P(=O)(O)O)P(=O)(O)O
FormulaC7 H11 N O7 P2
Name1-HYDROXY-2-(3-PYRIDINYL)ETHYLIDENE BIS-PHOSPHONIC ACID;
Risedronate
ChEMBLCHEMBL923
DrugBankDB00884
ZINCZINC000001531009
PDB chain4n9u Chain A Residue 404 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4n9u The role of lysine 200 in the human farnesyl pyrophosphate synthase catalytic mechanism and the mode of inhibition by the nitrogen-containing bisphosphonates
Resolution2.11 Å
Binding residue
(original residue number in PDB)		L100 D103 R112 Q171 G200 T201 D243 K257
Binding residue
(residue number reindexed from 1)		L89 D92 R101 Q160 G189 T190 D232 K246
Annotation score1
Binding affinityBindingDB: IC50=11nM,Ki=82.2nM
Enzymatic activity
Catalytic site (original residue number in PDB) K57 F98 D103 D107 R112 D174 G200 F239 D243 D244
Catalytic site (residue number reindexed from 1) K46 F87 D92 D96 R101 D163 G189 F228 D232 D233
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:4n9u, PDBe:4n9u, PDBj:4n9u
PDBsum4n9u
PubMed
UniProtP14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)

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