Structure of PDB 6n7y Chain F

Receptor sequence
>6n7yF (length=336) Species: 9606 (Homo sapiens) [Search protein sequence]
YAQEKQDFVQHFSQIVRVLTEGHPEIGDAIARLKEVLEYNAIGGKYNRGL
TVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTR
RGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQ
SSYQTEIGQTLDLLTAPNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAAAM
YMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTDIQD
NKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPAVF
LQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYK
3D structure
PDB6n7y Chirality-Driven Mode of Binding of alpha-Aminophosphonic Acid-Based Allosteric Inhibitors of the Human Farnesyl Pyrophosphate Synthase (hFPPS).
ChainF
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) K57 F98 D103 D107 R112 D174 K200 F239 D243 D244
Catalytic site (residue number reindexed from 1) K45 F86 D91 D95 R100 D162 K186 F225 D229 D230
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 KFA F N59 F206 F239 L246 L344 K347 N47 F192 F225 L232 L330 K333 MOAD: ic50=7.7uM
PDBbind-CN: -logKd/Ki=5.11,IC50=7.7uM
BindingDB: IC50=7700nM
BS02 PO4 F Q96 R113 Q84 R101
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:6n7y, PDBe:6n7y, PDBj:6n7y
PDBsum6n7y
PubMed31577901
UniProtP14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)

[Back to BioLiP]