Structure of PDB 5ksx Chain F

Receptor sequence
>5ksxF (length=339) Species: 9606 (Homo sapiens) [Search protein sequence]
VYAQEKQDFVQHFSQIVRVLTEGHPEIGDAIARLKEVLEYNAIGGKYNRG
LTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLT
RRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFL
QSSYQTEIGQTLDLLTAPQNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAA
AMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTDI
QDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPA
VFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYKR
3D structure
PDB5ksx Pharmacophore Mapping of Thienopyrimidine-Based Monophosphonate (ThP-MP) Inhibitors of the Human Farnesyl Pyrophosphate Synthase.
ChainF
Resolution2.65 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.5.1.1: dimethylallyltranstransferase.
2.5.1.10: (2E,6E)-farnesyl diphosphate synthase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 PO4 F G56 K57 R113 G45 K46 R102
BS02 7AM F E318 Y322 R346 Y349 K350 R351 E306 Y310 R334 Y337 K338 R339 PDBbind-CN: -logKd/Ki=5.43,IC50=3.7uM
BindingDB: IC50=3700nM
BS03 7AM F K57 N59 F239 R346 K347 I348 K350 K46 N48 F227 R334 K335 I336 K338 PDBbind-CN: -logKd/Ki=5.43,IC50=3.7uM
BindingDB: IC50=3700nM
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

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Molecular Function
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Biological Process
External links
PDB RCSB:5ksx, PDBe:5ksx, PDBj:5ksx
PDBsum5ksx
PubMed28208018
UniProtP14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)

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