Reaction Details |
| Report a problem with these data |
Target | Protein farnesyltransferase subunit beta/geranylgeranyltransferase type-1 subunit alpha |
---|
Ligand | BDBM50071241 |
---|
Substrate/Competitor | n/a |
---|
Meas. Tech. | ChEBML_161585 |
---|
IC50 | 13000±n/a nM |
---|
Citation | Singh, SB; Zink, DL; Williams, M; Polishook, JD; Sanchez, M; Silverman, KC; Lingham, RB Kampanols: novel Ras farnesyl-protein transferase inhibitors from Stachybotrys kampalensis. Bioorg Med Chem Lett8:2071-6 (1999) [PubMed] |
---|
More Info.: | Get all data from this article, Assay Method |
---|
|
Protein farnesyltransferase subunit beta/geranylgeranyltransferase type-1 subunit alpha |
---|
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: | MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFS
SYKFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQ
IVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYDIINREKLLQY
LYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIG
GVPGMEAHGGYTFCGLAALVILKRERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCY
SFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDF
YHTCYCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTYFLQKPV
PGFEELKDETSAEPATD
|
|
|
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: | MAATEGVGEAAQGGEPGQPAQPPPQPHPPPPQQQHKEEMAAEAGEAVASPMDDGFVSLDS
PSYVLYRDRAEWADIDPVPQNDGPNPVVQIIYSDKFRDVYDYFRAVLQRDERSERAFKLT
RDAIELNAANYTVWHFRRVLLKSLQKDLHEEMNYITAIIEEQPKNYQVWHHRRVLVEWLR
DPSQELEFIADILNQDAKNYHAWQHRQWVIQEFKLWDNELQYVDQLLKEDVRNNSVWNQR
YFVISNTTGYNDRAVLEREVQYTLEMIKLVPHNESAWNYLKGILQDRGLSKYPNLLNQLL
DLQPSHSSPYLIAFLVDIYEDMLENQCDNKEDILNKALELCEILAKEKDTIRKEYWRYIG
RSLQSKHSTENDSPTNVQQ
|
|
|
BDBM50071241 |
---|
n/a |
---|
Name | BDBM50071241 |
Synonyms: | Acetic acid (6aR,6bS,9S,10aR,12aS)-5-hydroxy-6b,10,10,12a-tetramethyl-3-oxo-3,6,6a,6b,7,8,9,10,10a,11,12,12a-dodecahydro-1H-2,13-dioxa-benzo[a]cyclopenta[h]anthracen-9-yl ester | CHEMBL62448 |
Type | Small organic molecule |
Emp. Form. | C25H32O6 |
Mol. Mass. | 428.518 |
SMILES | CC(=O)O[C@H]1CC[C@@]2(C)[C@@H](CC[C@]3(C)Oc4c5COC(=O)c5cc(O)c4C[C@H]23)C1(C)C |
Structure |
|