Detailed information for compound 1964159
Basic information
Technical information
- Name: Unnamed compound
- MW: 503.513 | Formula: C26H28F3N3O4
-
H donors: 3
H acceptors: 4
LogP: 3.21
Rotable bonds: 8
Rule of 5 violations (Lipinski): 2 - SMILES: NC(=O)C(n1ncc(c1)c1cc(OCCC(O)(C)C)cc2c1c1ccccc1[C@]2(O)C(F)(F)F)(C)C
- InChi: 1S/C26H28F3N3O4/c1-23(2,34)9-10-36-16-11-18(15-13-31-32(14-15)24(3,4)22(30)33)21-17-7-5-6-8-19(17)25(35,20(21)12-16)26(27,28)29/h5-8,11-14,34-35H,9-10H2,1-4H3,(H2,30,33)/t25-/m1/s1
- InChiKey: KNPYQCPWTWANOG-RUZDIDTESA-N
Network
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Synonyms
No synonyms found for this compound
Targets
Known targets for this compound
| Species | Target name | Source | Bibliographic reference |
|---|---|---|---|
| Homo sapiens | pyruvate dehydrogenase kinase, isozyme 2 | Starlite/ChEMBL | No references |
| Homo sapiens | pyruvate dehydrogenase kinase, isozyme 1 | Starlite/ChEMBL | No references |
Predicted pathogen targets for this compound
By orthology
By sequence similarity to non orthologous known druggable targets
| Species | Potential target | Known druggable target | Length | Alignment span | Identity |
|---|---|---|---|---|---|
| Trypanosoma brucei | pyruvate dehydrogenase (lipoamide) kinase, putative | pyruvate dehydrogenase kinase, isozyme 2 | 343 aa | 321 aa | 22.7 % |
| Leishmania major | pyruvate dehydrogenase (lipoamide) kinase, putative | pyruvate dehydrogenase kinase, isozyme 1 | 456 aa | 397 aa | 22.7 % |
Obtained from network model
Ranking Plot
Putative Targets List
| Species | Potential target | Raw | Global | Species |
|---|---|---|---|---|
| Toxoplasma gondii | ATPase/histidine kinase/DNA gyrase B/HSP90 domain-containing protein | 0.0116 | 0 | 0.5 |
| Schistosoma mansoni | pyruvate dehydrogenase | 0.0287 | 1 | 1 |
| Leishmania major | developmentally regulated phosphoprotein-like protein | 0.0287 | 1 | 0.5 |
| Echinococcus multilocularis | Pyruvate dehydrogenase (lipoamide) kinase | 0.0287 | 1 | 0.5 |
| Loa Loa (eye worm) | hypothetical protein | 0.0287 | 1 | 0.5 |
| Trypanosoma brucei | developmentally regulated phosphoprotein | 0.0287 | 1 | 0.5 |
| Echinococcus multilocularis | Pyruvate dehydrogenase (lipoamide) kinase | 0.0287 | 1 | 0.5 |
| Echinococcus granulosus | Pyruvate dehydrogenase lipoamide kinase | 0.0287 | 1 | 0.5 |
| Trypanosoma cruzi | developmentally regulated phosphoprotein, putative | 0.0287 | 1 | 0.5 |
Activities
| Activity type | Activity value | Assay description | Source | Reference |
|---|---|---|---|---|
| IC50 (binding) | = 4.6 nM | BindingDB_Patents: Inhbition Assay. For expression of hPDHK2 activity, Escherichia coli strain BL21(DE3) cells (Novagen) were transformed with the pET17b vector containing modified hPDHK2 cDNA. The Escherichia coli were grown to an optical density 0.6 (600 nmol/L) at 30 C. Protein expression was induced by the addition of 500 umol/L isopropyl-beta -thiogalactopyranoside. The Escherichia coli were cultured at 30 C. for 5 hr and harvested by centrifugation. Resuspension of the Escherichia coli paste was disrupted by a microfluidizer. FLAG-Tagged protein was purified using FLAG affinity gel. The gel was washed with 20 mmol/L HEPES-NaOH, 500 mmol/L sodium chloride, 1% ethylene glycol, and 0.1% Pluronic F-68 (pH 8.0), and the binding protein was eluted with 20 mmol/L HEPES-NaOH, 100 ug/mL FLAG peptide, 500 mmol/L sodium chloride, 1% ethylene glycol, and 0.1% Pluronic F-68 (pH 8.0). The eluted fractions containing FLAG-Tagged protein were pooled, dialyzed against 20 mmol/L HEPES-NaOH, 150 mmol/L sodium chloride. | ChEMBL. | No reference |
| IC50 (binding) | = 4.6 nM | BindingDB_Patents: Inhbition Assay. For expression of hPDHK2 activity, Escherichia coli strain BL21(DE3) cells (Novagen) were transformed with the pET17b vector containing modified hPDHK2 cDNA. The Escherichia coli were grown to an optical density 0.6 (600 nmol/L) at 30 C. Protein expression was induced by the addition of 500 umol/L isopropyl-beta -thiogalactopyranoside. The Escherichia coli were cultured at 30 C. for 5 hr and harvested by centrifugation. Resuspension of the Escherichia coli paste was disrupted by a microfluidizer. FLAG-Tagged protein was purified using FLAG affinity gel. The gel was washed with 20 mmol/L HEPES-NaOH, 500 mmol/L sodium chloride, 1% ethylene glycol, and 0.1% Pluronic F-68 (pH 8.0), and the binding protein was eluted with 20 mmol/L HEPES-NaOH, 100 ug/mL FLAG peptide, 500 mmol/L sodium chloride, 1% ethylene glycol, and 0.1% Pluronic F-68 (pH 8.0). The eluted fractions containing FLAG-Tagged protein were pooled, dialyzed against 20 mmol/L HEPES-NaOH, 150 mmol/L sodium chloride. | ChEMBL. | No reference |
| IC50 (binding) | = 4.7 nM | BindingDB_Patents: Inhbition Assay. For expression of hPDHK1 activity, Escherichia coli strain BL21(DE3) cells (Novagen) were transformed with the pET17b vector containing modified hPDHK1 cDNA. The Escherichia coli were grown to an optical density 0.6 (600 nmol/L) at 30° C. Protein expression was induced by the addition of 500 µmol/L isopropyl-ß-thiogalactopyranoside. The Escherichia coli were cultured at 30° C. for 5 hr and harvested by centrifugation. Resuspension of the Escherichia coli paste was disrupted by a microfluidizer. FLAG-Tagged protein was purified using FLAG affinity gel (Sigma).The gel was washed with 20 mmol/L N-(2-hydroxyethyl)piperazine-N'-2-ethanesulfonic acid-sodium hydroxide (HEPES-NaOH), 500 mmol/L sodium chloride, 1% ethylene glycol, and 0.1% polyoxyethylene-polyoxypropylene block copolymer (Pluronic F-68, pH 8.0), and the binding protein was eluted with 20 mmol/L HEPES-NaOH, 100 µg/mL FLAG peptide, 500 mmol/L sodium chloride, 1% ethylene glycol, and 0.1% Pluronic F-68 (pH 8. | ChEMBL. | No reference |
| IC50 (binding) | = 4.7 nM | BindingDB_Patents: Inhbition Assay. For expression of hPDHK1 activity, Escherichia coli strain BL21(DE3) cells (Novagen) were transformed with the pET17b vector containing modified hPDHK1 cDNA. The Escherichia coli were grown to an optical density 0.6 (600 nmol/L) at 30° C. Protein expression was induced by the addition of 500 µmol/L isopropyl-ß-thiogalactopyranoside. The Escherichia coli were cultured at 30° C. for 5 hr and harvested by centrifugation. Resuspension of the Escherichia coli paste was disrupted by a microfluidizer. FLAG-Tagged protein was purified using FLAG affinity gel (Sigma).The gel was washed with 20 mmol/L N-(2-hydroxyethyl)piperazine-N'-2-ethanesulfonic acid-sodium hydroxide (HEPES-NaOH), 500 mmol/L sodium chloride, 1% ethylene glycol, and 0.1% polyoxyethylene-polyoxypropylene block copolymer (Pluronic F-68, pH 8.0), and the binding protein was eluted with 20 mmol/L HEPES-NaOH, 100 µg/mL FLAG peptide, 500 mmol/L sodium chloride, 1% ethylene glycol, and 0.1% Pluronic F-68 (pH 8. | ChEMBL. | No reference |
| IC50 (binding) | = 4.9 nM | BindingDB_Patents: Inhbition Assay. For expression of hPDHK2 activity, Escherichia coli strain BL21(DE3) cells (Novagen) were transformed with the pET17b vector containing modified hPDHK2 cDNA. The Escherichia coli were grown to an optical density 0.6 (600 nmol/L) at 30 C. Protein expression was induced by the addition of 500 umol/L isopropyl-beta -thiogalactopyranoside. The Escherichia coli were cultured at 30 C. for 5 hr and harvested by centrifugation. Resuspension of the Escherichia coli paste was disrupted by a microfluidizer. FLAG-Tagged protein was purified using FLAG affinity gel. The gel was washed with 20 mmol/L HEPES-NaOH, 500 mmol/L sodium chloride, 1% ethylene glycol, and 0.1% Pluronic F-68 (pH 8.0), and the binding protein was eluted with 20 mmol/L HEPES-NaOH, 100 ug/mL FLAG peptide, 500 mmol/L sodium chloride, 1% ethylene glycol, and 0.1% Pluronic F-68 (pH 8.0). The eluted fractions containing FLAG-Tagged protein were pooled, dialyzed against 20 mmol/L HEPES-NaOH, 150 mmol/L sodium chloride. | ChEMBL. | No reference |
| IC50 (binding) | = 4.9 nM | BindingDB_Patents: Inhbition Assay. For expression of hPDHK2 activity, Escherichia coli strain BL21(DE3) cells (Novagen) were transformed with the pET17b vector containing modified hPDHK2 cDNA. The Escherichia coli were grown to an optical density 0.6 (600 nmol/L) at 30 C. Protein expression was induced by the addition of 500 umol/L isopropyl-beta -thiogalactopyranoside. The Escherichia coli were cultured at 30 C. for 5 hr and harvested by centrifugation. Resuspension of the Escherichia coli paste was disrupted by a microfluidizer. FLAG-Tagged protein was purified using FLAG affinity gel. The gel was washed with 20 mmol/L HEPES-NaOH, 500 mmol/L sodium chloride, 1% ethylene glycol, and 0.1% Pluronic F-68 (pH 8.0), and the binding protein was eluted with 20 mmol/L HEPES-NaOH, 100 ug/mL FLAG peptide, 500 mmol/L sodium chloride, 1% ethylene glycol, and 0.1% Pluronic F-68 (pH 8.0). The eluted fractions containing FLAG-Tagged protein were pooled, dialyzed against 20 mmol/L HEPES-NaOH, 150 mmol/L sodium chloride. | ChEMBL. | No reference |
| IC50 (binding) | = 6.6 nM | BindingDB_Patents: Inhbition Assay. For expression of hPDHK1 activity, Escherichia coli strain BL21(DE3) cells (Novagen) were transformed with the pET17b vector containing modified hPDHK1 cDNA. The Escherichia coli were grown to an optical density 0.6 (600 nmol/L) at 30° C. Protein expression was induced by the addition of 500 µmol/L isopropyl-ß-thiogalactopyranoside. The Escherichia coli were cultured at 30° C. for 5 hr and harvested by centrifugation. Resuspension of the Escherichia coli paste was disrupted by a microfluidizer. FLAG-Tagged protein was purified using FLAG affinity gel (Sigma).The gel was washed with 20 mmol/L N-(2-hydroxyethyl)piperazine-N'-2-ethanesulfonic acid-sodium hydroxide (HEPES-NaOH), 500 mmol/L sodium chloride, 1% ethylene glycol, and 0.1% polyoxyethylene-polyoxypropylene block copolymer (Pluronic F-68, pH 8.0), and the binding protein was eluted with 20 mmol/L HEPES-NaOH, 100 µg/mL FLAG peptide, 500 mmol/L sodium chloride, 1% ethylene glycol, and 0.1% Pluronic F-68 (pH 8. | ChEMBL. | No reference |
| IC50 (binding) | = 6.6 nM | BindingDB_Patents: Inhbition Assay. For expression of hPDHK1 activity, Escherichia coli strain BL21(DE3) cells (Novagen) were transformed with the pET17b vector containing modified hPDHK1 cDNA. The Escherichia coli were grown to an optical density 0.6 (600 nmol/L) at 30° C. Protein expression was induced by the addition of 500 µmol/L isopropyl-ß-thiogalactopyranoside. The Escherichia coli were cultured at 30° C. for 5 hr and harvested by centrifugation. Resuspension of the Escherichia coli paste was disrupted by a microfluidizer. FLAG-Tagged protein was purified using FLAG affinity gel (Sigma).The gel was washed with 20 mmol/L N-(2-hydroxyethyl)piperazine-N'-2-ethanesulfonic acid-sodium hydroxide (HEPES-NaOH), 500 mmol/L sodium chloride, 1% ethylene glycol, and 0.1% polyoxyethylene-polyoxypropylene block copolymer (Pluronic F-68, pH 8.0), and the binding protein was eluted with 20 mmol/L HEPES-NaOH, 100 µg/mL FLAG peptide, 500 mmol/L sodium chloride, 1% ethylene glycol, and 0.1% Pluronic F-68 (pH 8. | ChEMBL. | No reference |
Phenotypes
Whole-cell/tissue/organism interactions
We have no records of whole-cell/tissue assays done with this compound
What does this mean?
Many chemical entities in TDR Targets come from high-throughput screenings with whole cells or tissue samples, and not all assayed compounds have been tested against a single a single target protein, probably because they get ruled out during screening process. Even if these compounds may have not been of interest in the original screening, they may come as interesting leads for other screening assays. Furthermore, we may be able to propose drug-target associations using chemical similarities and network patterns.
Annotated phenotypes:
We have no manually annotated phenotypes for this drug.
What does this mean? / Care to help?
In TDR Targets, information about phenotypes that are caused by
drugs, or by genetic manipulation of cells (e.g. gene knockouts or
knockdowns) is manually curated from the literature. These
descriptions help to describe the potential of the target for drug
development. If no information is available for this gene or if the
information is incomplete, this may mean that i) the papers
containing this information either appeared after the curation
effort for this organism was carried out or they were inadvertently
missed by curators; or that ii) the curation effort for this
organism has not yet started.
In any case, if you have information about papers containing relevant validation data for this target, please log in using your TDR Targets username and password and send them to us using the corresponding form in this page (only visible to registered users) or contact us.
In any case, if you have information about papers containing relevant validation data for this target, please log in using your TDR Targets username and password and send them to us using the corresponding form in this page (only visible to registered users) or contact us.
External resources for this compound
- ChEMBL: CHEMBL3673096
Bibliographic References
No literature references available for this target.
If you have references for this compound, please enter them in a user comment (below) or Contact us.