Structure of PDB 4q23 Chain A Binding Site BS01

Receptor Information
>4q23 Chain A (length=337) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
VYAQEKQDFVQHFSQIVRVLTGHPEIGDAIARLKEVLEYNAIGGKYNRGL
TVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTR
RGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQ
SSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKAAFYSFYLPIAA
AMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTDI
QDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPA
VFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIY
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 chain4q23 Chain A Residue 901 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4q23 The role of threonine 201 and tyrosine 204 in the human farnesyl pyrophosphate synthase catalytic mechanism and the mode of inhibition by the nitrogen-containing bisphosphonates
Resolution1.98 Å
Binding residue
(original residue number in PDB)		L100 D103 R112 Q171 K200 D243 K257
Binding residue
(residue number reindexed from 1)		L88 D91 R100 Q159 K188 D231 K245
Annotation score1
Binding affinityBindingDB: IC50=11nM,Ki=82.2nM
Enzymatic activity
Catalytic site (original residue number in PDB) K57 F98 D103 D107 R112 D174 K200 F239 D243 D244
Catalytic site (residue number reindexed from 1) K45 F86 D91 D95 R100 D162 K188 F227 D231 D232
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:4q23, PDBe:4q23, PDBj:4q23
PDBsum4q23
PubMed
UniProtP14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)

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