Structure of PDB 4ogu Chain A Binding Site BS04

Receptor Information
>4ogu Chain A (length=339) Species: 9606 (Homo sapiens) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DVYAQEKQDFVQHFSQIVRVLTEHPEIGDAIARLKEVLEYNTIGGKYNRG
LTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLT
RRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFL
QSSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPIA
AAMYMAGIDGEKEHANAKKILLEMGEFAQIQDDYLDLFGDPSVTGKIGTD
IQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLP
AVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYK
Ligand information
Ligand ID210
InChIInChI=1S/C3H11NO7P2/c4-2-1-3(5,12(6,7)8)13(9,10)11/h5H,1-2,4H2,(H2,6,7,8)(H2,9,10,11)
InChIKeyWRUUGTRCQOWXEG-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341NCCC(O)([P](O)(O)=O)[P](O)(O)=O
ACDLabs 10.04O=P(O)(O)C(O)(CCN)P(=O)(O)O
OpenEye OEToolkits 1.5.0C(CN)C(O)(P(=O)(O)O)P(=O)(O)O
FormulaC3 H11 N O7 P2
NamePAMIDRONATE;
(3-AMINO-1-HYDROXY-1-PHOSPHONO-PROPYL)PHOSPHONIC ACID
ChEMBLCHEMBL834
DrugBankDB00282
ZINCZINC000003812862
PDB chain4ogu Chain A Residue 405 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB4ogu The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates
Resolution2.1 Å
Binding residue
(original residue number in PDB)		D103 R112 K200 Q240 D243 K257
Binding residue
(residue number reindexed from 1)		D92 R101 K189 Q229 D232 K246
Annotation score1
Binding affinityBindingDB: IC50=200nM,Ki=55.9nM
Enzymatic activity
Catalytic site (original residue number in PDB) K57 F98 D103 D107 R112 D174 K200 A239 D243 D244
Catalytic site (residue number reindexed from 1) K46 F87 D92 D96 R101 D163 K189 A228 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:4ogu, PDBe:4ogu, PDBj:4ogu
PDBsum4ogu
PubMed
UniProtP14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)

[Back to BioLiP]