Structure of PDB 4nkf Chain A

Receptor sequence

>4nkfA (length=339) Species: 9606 (Homo sapiens)

DVYAQEKQDFVQHFSQIVRVLTEHPEIGDAIARLKEVLEYNTIGGKYNRG
LTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLT
RRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFL
QSSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPIA
AAMYMAGIDGEKEHANAKKILLEMGEFAQIQDDYLDLFGDPSVTGKIGTD
IQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLP
AVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYK

3D structure

• PDB: 4nkf The effects of Lysine 200 and Phenylalanine 239 Farnesyl Pyrophosphate Synthase (FPPS) mutations on the catalytic activity, crystal structure and inhibition by nitrogen containing bisphosphonates
• Chain: A
• Resolution: 2.0 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K57 F98 D103 D107 R112 D174 K200 A239 D243 D244
• Catalytic site (residue number reindexed from 1): K46 F87 D92 D96 R101 D163 K189 A228 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	210	A	D103 R112 K200 D243 K257	D92 R101 K189 D232 K246	BindingDB: IC50=200nM,Ki=55.9nM

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