Structure of PDB 2opm Chain A Binding Site BS03

Receptor Information

>2opm Chain A (length=336) Species: 9606 (Homo sapiens)

EKQDFVQHFSQIVRVLTEDEHPEIGDAIARLKEVLEYNAIGGKYNRGLTV
VVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMDSSLTRRG
QICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLIELFLQSS
YQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFYLPIAAAM
YMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGKIGTDIQD
NKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEELDLPAVF
LQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYK

Ligand information

• Ligand ID: MG
• InChI: InChI=1S/Mg/q+2
• InChIKey: JLVVSXFLKOJNIY-UHFFFAOYSA-N
• SMILES:
  ACDLabs 10.04
  OpenEye OEToolkits 1.5.0: [Mg+2]
  CACTVS 3.341: [Mg++]
• Formula: Mg
• Name: MAGNESIUM ION
• DrugBank: DB01378
• PDB chain: 2opm Chain A Residue 907

Receptor-Ligand Complex Structure

Structure summary

• PDB: 2opm Lipophilic bisphosphonates as dual farnesyl/geranylgeranyl diphosphate synthase inhibitors: an X-ray and NMR investigation.
• Resolution: 2.4 Å
• Binding residue (original residue number in PDB): D117 D121
• Binding residue (residue number reindexed from 1): D89 D93
• Annotation score: 1

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.

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)