Structure of PDB 2opm Chain A

Receptor sequence

>2opmA (length=336) Species: 9606 (Homo sapiens)

EKQDFVQHFSQIVRVLTEDEHPEIGDAIARLKEVLEYNAIGGKYNRGLTV
VVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRG
QICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQSS
YQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAAAM
YMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTDIQD
NKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPAVF
LQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYK

3D structure

• PDB: 2opm Lipophilic bisphosphonates as dual farnesyl/geranylgeranyl diphosphate synthase inhibitors: an X-ray and NMR investigation.
• Chain: A
• Resolution: 2.4 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): K71 F112 D117 D121 R126 D188 K214 F253 D257 D258
• Catalytic site (residue number reindexed from 1): K43 F84 D89 D93 R98 D160 K186 F225 D229 D230
• 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	PO4	A	G70 K71 Q110 R127	G42 K43 Q82 R99
BS02	PO4	A	K71 R74 Q110	K43 R46 Q82
BS03	MG	A	D117 D121	D89 D93
BS04	MG	A	D117 D121	D89 D93
BS05	NI9	A	D117 R126 K214 T215 Q254 D257 K271	D89 R98 K186 T187 Q226 D229 K243

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:2opm, PDBe:2opm, PDBj:2opm
• PDBsum: 2opm
• PubMed: 19309137
• UniProt: P14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)