Structure of PDB 5jv1 Chain F

Receptor sequence
>5jv1F (length=336) Species: 9606 (Homo sapiens) [Search protein sequence]
VYAQEKQDFVQHFSQIVRVLTEHPEIGDAIARLKEVLEYNAIGGKYNRGL
TVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTR
RGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQ
SSYQTEIGQTLDLLTAPNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAAAM
YMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTDIQD
NKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPAVF
LQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYK
3D structure
PDB5jv1 Pharmacophore Mapping of Thienopyrimidine-Based Monophosphonate (ThP-MP) Inhibitors of the Human Farnesyl Pyrophosphate Synthase.
ChainF
Resolution2.3 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 YL6 F K57 N59 R60 S205 F206 F239 Q242 D243 K45 N47 R48 S191 F192 F225 Q228 D229 MOAD: ic50=0.86uM
PDBbind-CN: -logKd/Ki=6.07,IC50=0.86uM
BS02 YL6 F E319 Y322 A345 R346 Y349 K350 E305 Y308 A331 R332 Y335 K336 MOAD: ic50=0.86uM
PDBbind-CN: -logKd/Ki=6.07,IC50=0.86uM
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:5jv1, PDBe:5jv1, PDBj:5jv1
PDBsum5jv1
PubMed28208018
UniProtP14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)

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