Structure of PDB 5jv2 Chain F

Receptor sequence
>5jv2F (length=331) Species: 9606 (Homo sapiens) [Search protein sequence]
YAQEKQDFVQHFSQIVRVLTEPEIGDAIARLKEVLEYNAIGGKYNRGLTV
VVAFRELVPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRGQ
ICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQSSY
QTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAAAMY
MAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPKIGTDIQDNKCSW
LVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPAVFLQYEE
DSYSHIMALIEQYAAPLPPAVFLGLARKIYK
3D structure
PDB5jv2 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 PO4 F G56 K57 R113 G42 K43 R98
BS02 6O3 F N59 F239 L344 K347 N45 F224 L325 K328 MOAD: ic50~100uM
PDBbind-CN: -logKd/Ki=4.00,IC50~100uM
BS03 6O3 F Y322 R346 Y303 R327 MOAD: ic50~100uM
PDBbind-CN: -logKd/Ki=4.00,IC50~100uM
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:5jv2, PDBe:5jv2, PDBj:5jv2
PDBsum5jv2
PubMed28208018
UniProtP14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)

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