Structure of PDB 6oag Chain F

Receptor sequence

>6oagF (length=343) Species: 9606 (Homo sapiens)

DVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAIGGK
YNRGLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMD
SSLTRRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLI
ELFLQSSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFY
LPIAAAMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGK
IGTDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEE
LDLPAVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYK

3D structure

• PDB: 6oag Chirality-Driven Mode of Binding of alpha-Aminophosphonic Acid-Based Allosteric Inhibitors of the Human Farnesyl Pyrophosphate Synthase (hFPPS).
• Chain: F
• Resolution: 2.3 Å

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): K50 F91 D96 D100 R105 D167 K193 F232 D236 D237
• 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	M2Y	F	K57 N59 F206 F239 D243	K50 N52 F199 F232 D236	MOAD: ic50=3.7uM PDBbind-CN: -logKd/Ki=5.43,IC50=3.7uM
BS02	M2Y	F	E318 Y322 Y349 K350	E311 Y315 Y342 K343	MOAD: ic50=3.7uM PDBbind-CN: -logKd/Ki=5.43,IC50=3.7uM
BS03	PO4	F	G56 Q96 R113	G49 Q89 R106

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

External links

• PDB: RCSB:6oag, PDBe:6oag, PDBj:6oag
• PDBsum: 6oag
• PubMed: 31577901
• UniProt: P14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)