Structure of PDB 4nke Chain A

Receptor sequence

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

VYAQEKQDFVQHFSQIVRVLTEHPEIGDAIARLKEVLEYNTIGGKYNRGL
TVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTR
RGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQ
SSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAA
AMYMAGIDGEKEHANAKKILLEMGEFAQIQDDYLDLFGDPSVTGKIGTDI
QDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPA
VFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYK

3D structure

• PDB: 4nke 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: 1.46 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): K45 F86 D91 D95 R100 D162 K188 A227 D231 D232
• 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	D91 D95
BS02	MG	A	D103 D107	D91 D95
BS03	RIS	A	D103 R112 Q171 K200 T201 D243 K257	D91 R100 Q159 K188 T189 D231 K245	BindingDB: IC50=11nM,Ki=82.2nM
BS04	IPE	A	G56 K57 R60 Q96 R113 T201 D243	G44 K45 R48 Q84 R101 T189 D231

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