Reaction Details Report a problem with these data
Target
Protein farnesyltransferase subunit beta/geranylgeranyltransferase type-1 subunit alpha
Ligand
BDBM50101929
Substrate
n/a
Meas. Tech.
ChEBML_70719
IC50
0.290000±n/a nM
Citation
 Dinsmore, CJ; Zartman, CB; Bergman, JM; Abrams, MT; Buser, CA; Culberson, JC; Davide, JP; Ellis-Hutchings, M; Fernandes, C; Graham, SL; Hartman, GD; Huber, HE; Lobell, RB; Mosser, SD; Robinson, RG; Williams, TM Macrocyclic piperazinones as potent dual inhibitors of farnesyltransferase and geranylgeranyltransferase-I. Bioorg Med Chem Lett 14:639-43 (2004) [PubMed]  Article 
Target
Name:
Protein farnesyltransferase subunit beta/geranylgeranyltransferase type-1 subunit alpha
Synonyms:
Farnesyltransferase (FTase) | Protein Farnesyltransferase (PFT) | Protein Farnesyltransferase (PFT) Chain B | Protein farnesyltransferase
Type:
Protein Complex
Mol. Mass.:
n/a
Description:
To express recombinant enzyme in E. coli, the cloned human alpha and beta subunits were co-expressed from a plasmid, in which their expression was translationally coupled.
Components:
This complex has 2 components.
Component 1
Name:
Protein farnesyltransferase subunit beta
Synonyms:
CAAX farnesyltransferase subunit alpha | CAAX farnesyltransferase subunit beta | FNTB | FNTB_HUMAN | FTase-alpha | FTase-beta | GGTase-I-alpha | Protein Farnesyltransferase (PFT) Chain B | Protein farnesyl/geranylgeranyl transferase | Protein farnesyltransferase beta subunit | Protein farnesyltransferase subunit beta | Protein farnesyltransferase/geranylgeranyltransferase type I alpha subunit | Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha | Ras proteins prenyltransferase subunit alpha | Ras proteins prenyltransferase subunit beta | Type I protein geranyl-geranyltransferase subunit alpha
Type:
Enzyme Subunit
Mol. Mass.:
48766.02
Organism:
Homo sapiens (Human)
Description:
Protein farnesyltransferase subunit beta
Residue:
437
Sequence:
MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQIVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYDIINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKRERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTYFLQKPVPGFEELKDETSAEPATD
  
Component 2
Name:
Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
Synonyms:
CAAX farnesyltransferase alpha subunit | FNTA | FNTA_HUMAN | FTase-1-alpha | FTase-alpha | GGTase-I-alpha | Geranylgeranyl Transferase (GGTase-I) Chain A | Geranylgeranyl transferase type I | Protein Farnesyltransferase (PFT) Chain A | Protein farnesyl/geranylgeranyl transferase | Protein farnesyltransferase | Protein farnesyltransferase subunit alpha | Protein farnesyltransferase/geranylgeranyltransferase type I alpha subunit | Ras proteins prenyltransferase alpha
Type:
Enzyme
Mol. Mass.:
44392.46
Organism:
Homo sapiens (Human)
Description:
Recombinant human FTase.
Residue:
379
Sequence:
MAATEGVGEAAQGGEPGQPAQPPPQPHPPPPQQQHKEEMAAEAGEAVASPMDDGFVSLDSPSYVLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLTRDAIELNAANYTVWHFRRVLLKSLQKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLRDPSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQYVDQLLKEDVRNNSVWNQRYFVISNTTGYNDRAVLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSKYPNLLNQLLDLQPSHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKEYWRYIGRSLQSKHSTENDSPTNVQQ
  
Inhibitor
Name:
BDBM50101929
Synonyms:
3-oxo-18-oxa-2,5,9,11-tetraazahexacyclo[17.6.2.22,5.113,17.07,11.022,26]triaconta-1(26),7,9,13(30),14,16,19(27),20,22,24-decaen-16-yl cyanide | 3-oxo-18-oxa-2,5,9,11-tetraazahexacyclo[17.6.2.22,5.113,17.07,11.022,26]triaconta-1(26),7,9,13,15,17(30),19(27),20,22,24-decaen-16-yl cyanide | 4-{5-[4-(3-Chloro-phenyl)-3-oxo-piperazin-1-ylmethyl]-imidazol-1-ylmethyl}-benzonitrile | CHEMBL52073
Type:
Small organic molecule
Emp. Form.:
C26H21N5O2
Mol. Mass.:
435.4772
SMILES:
O=C1CN2CCN1c1cccc3ccc(Oc4cc(Cn5cncc5C2)ccc4C#N)cc13
Structure:
Search PDB for entries with ligand similarity: