Structure of PDB 4nke Chain A Binding Site BS04

Receptor Information
>4nke 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]
VYAQEKQDFVQHFSQIVRVLTEHPEIGDAIARLKEVLEYNTIGGKYNRGL
TVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTR
RGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQ
SSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAA
AMYMAGIDGEKEHANAKKILLEMGEFAQIQDDYLDLFGDPSVTGKIGTDI
QDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPA
VFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYK
Ligand information
Ligand IDIPE
InChIInChI=1S/C5H12O7P2/c1-5(2)3-4-11-14(9,10)12-13(6,7)8/h1,3-4H2,2H3,(H,9,10)(H2,6,7,8)
InChIKeyNUHSROFQTUXZQQ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341CC(=C)CCO[P](O)(=O)O[P](O)(O)=O
OpenEye OEToolkits 1.5.0CC(=C)CCOP(=O)(O)OP(=O)(O)O
ACDLabs 10.04O=P(OP(=O)(O)O)(OCC\C(=C)C)O
OpenEye OEToolkits 1.5.0CC(=C)CCO[P@@](=O)(O)OP(=O)(O)O
CACTVS 3.341CC(=C)CCO[P@](O)(=O)O[P](O)(O)=O
FormulaC5 H12 O7 P2
Name3-METHYLBUT-3-ENYL TRIHYDROGEN DIPHOSPHATE;
ISOPENTENYL PYROPHOSPHATE
ChEMBLCHEMBL356362
DrugBankDB04714
ZINCZINC000008215654
PDB chain4nke 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]
PDB4nke 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
Resolution1.46 Å
Binding residue
(original residue number in PDB)		G56 K57 R60 Q96 R113 T201 D243
Binding residue
(residue number reindexed from 1)		G44 K45 R48 Q84 R101 T189 D231
Annotation score5
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) K45 F86 D91 D95 R100 D162 K188 A227 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:4nke, PDBe:4nke, PDBj:4nke
PDBsum4nke
PubMed
UniProtP14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)

[Back to BioLiP]