Structure of PDB 4h5c Chain F Binding Site BS02

Receptor Information

>4h5c Chain F (length=346) Species: 9606 (Homo sapiens)

DVYAQEKQDFVQHFSQIVRVLTEDEMGHPEIGDAIARLKEVLEYNAIGGK
YNRGLTVVVAFRELVEPRKQDADSLQRAWTVGWCVELLQAFFLVADDIMD
SSLTRRGQICWYQKPGVGLDAINDANLLEACIYRLLKLYCREQPYYLNLI
ELFLQSSYQTEIGQTLDLLTAPQGNVDLVRFTEKRYKSIVKYKTAFYSFY
LPIAAAMYMAGIDGEKEHANAKKILLEMGEFFQIQDDYLDLFGDPSVTGK
IGTDIQDNKCSWLVVQCLQRATPEQYQILKENYGQKEAEKVARVKALYEE
LDLPAVFLQYEEDSYSHIMALIEQYAAPLPPAVFLGLARKIYKRRK

Ligand information

• Ligand ID: PO4
• InChI: InChI=1S/H3O4P/c1-5(2,3)4/h(H3,1,2,3,4)/p-3
• InChIKey: NBIIXXVUZAFLBC-UHFFFAOYSA-K
• SMILES:
  CACTVS 3.341: [O-][P]([O-])([O-])=O
  ACDLabs 10.04: [O-]P([O-])([O-])=O
  OpenEye OEToolkits 1.5.0: [O-]P(=O)([O-])[O-]
• Formula: O4 P
• Name: PHOSPHATE ION
• DrugBank: DB14523
• PDB chain: 4h5c Chain F Residue 402

Receptor-Ligand Complex Structure

Structure summary

• PDB: 4h5c Ternary complex structures of human farnesyl pyrophosphate synthase bound with a novel inhibitor and secondary ligands provide insights into the molecular details of the enzyme's active site closure.
• Resolution: 2.02 Å
• Binding residue (original residue number in PDB): G56 K57 R60 R113
• Binding residue (residue number reindexed from 1): G49 K50 R53 R106
• Annotation score: 1

Enzymatic activity

• 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:4h5c, PDBe:4h5c, PDBj:4h5c
• PDBsum: 4h5c
• PubMed: 23234314
• UniProt: P14324|FPPS_HUMAN Farnesyl pyrophosphate synthase (Gene Name=FDPS)