Structure of PDB 4ogu Chain A

Receptor sequence

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

DVYAQEKQDFVQHFSQIVRVLTEHPEIGDAIARLKEVLEYNTIGGKYNRG
LTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLT
RRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFL
QSSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPIA
AAMYMAGIDGEKEHANAKKILLEMGEFAQIQDDYLDLFGDPSVTGKIGTD
IQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLP
AVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYK

3D structure

• PDB: 4ogu 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: 2.1 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	IPE	A	K57 R60 Q96 R113 D243	K46 R49 Q85 R102 D232
BS04	210	A	D103 R112 K200 Q240 D243 K257	D92 R101 K189 Q229 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:4ogu, PDBe:4ogu, PDBj:4ogu
• PDBsum: 4ogu
• UniProt: P14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)