Structure of PDB 4n9u Chain A

Receptor sequence

>4n9uA (length=338) Species: 9606 (Homo sapiens)

DVYAQEKQDFVQHFSQIVRVLTEHPEIGDAIARLKEVLEYNTIGGKYNRG
LTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLT
RRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFL
QSSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYGTAFYSFYLPIA
AAMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTD
IQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLP
AVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIY

3D structure

• PDB: 4n9u The role of lysine 200 in the human farnesyl pyrophosphate synthase catalytic mechanism and the mode of inhibition by the nitrogen-containing bisphosphonates
• Chain: A
• Resolution: 2.11 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K57 F98 D103 D107 R112 D174 G200 F239 D243 D244
• Catalytic site (residue number reindexed from 1): K46 F87 D92 D96 R101 D163 G189 F228 D232 D233
• 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	MG	A	D103 D107	D92 D96
BS02	MG	A	D103 D107	D92 D96
BS03	RIS	A	L100 D103 R112 Q171 G200 T201 D243 K257	L89 D92 R101 Q160 G189 T190 D232 K246	BindingDB: IC50=11nM,Ki=82.2nM

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:4n9u, PDBe:4n9u, PDBj:4n9u
• PDBsum: 4n9u
• UniProt: P14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)