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compound ax20017  (MedChemExpress)
94
MedChemExpress compound ax20017
Structure of the <t>PknG-AX20017</t> complex (ID PDB: 2PZI ). (A) Ribbon representation of the PknG kinase domain. Typical secondary structure elements are indicated: DLG motif is colored black, P-loop is colored pink, activation loop is colored yellow, the catalytic loop is colored red, and helix C is colored green. The binding pocket of inhibitor AX20017 is shown in light blue. (B) Interacting residues are shown. Inhibitor AX20017 is shown in gray color. Residues Glu233 and Val235 form hydrogen bonds.
Compound Ax20017, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 94/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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Average 94 stars, based on 1 article reviews
compound ax20017 - by Bioz Stars, 2026-02
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bms-502  (MedChemExpress)
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BMS-502 (Compound 22) is a potent dual inhibitor of diacylglycerol kinase (DGK) α and ζ with IC50 of 4.6 nM and 2.1 nM. BMS-502 enhanced T cell immune responses in mice. BMS-502 can be used
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Image Search Results


Structure of the PknG-AX20017 complex (ID PDB: 2PZI ). (A) Ribbon representation of the PknG kinase domain. Typical secondary structure elements are indicated: DLG motif is colored black, P-loop is colored pink, activation loop is colored yellow, the catalytic loop is colored red, and helix C is colored green. The binding pocket of inhibitor AX20017 is shown in light blue. (B) Interacting residues are shown. Inhibitor AX20017 is shown in gray color. Residues Glu233 and Val235 form hydrogen bonds.

Journal: ACS Omega

Article Title: Identifying RO9021 as a Potential Inhibitor of PknG from Mycobacterium tuberculosis : Combinative Computational and In Vitro Studies

doi: 10.1021/acsomega.2c02093

Figure Lengend Snippet: Structure of the PknG-AX20017 complex (ID PDB: 2PZI ). (A) Ribbon representation of the PknG kinase domain. Typical secondary structure elements are indicated: DLG motif is colored black, P-loop is colored pink, activation loop is colored yellow, the catalytic loop is colored red, and helix C is colored green. The binding pocket of inhibitor AX20017 is shown in light blue. (B) Interacting residues are shown. Inhibitor AX20017 is shown in gray color. Residues Glu233 and Val235 form hydrogen bonds.

Article Snippet: Compound AX20017 was received from the MedChem Express Library (MCE; Monmouth Junction, NJ); and the CHEMBL compounds were received from Chemspace US Inc. (Chemspace; Monmouth Junction, NJ 08852).

Techniques: Activation Assay, Binding Assay

Binding modes of inhibitor AX20017 and THBT derivatives. (A) X-ray reference structure of AX20017 (in gray) (PDB ID: 2PZI ) and docked conformations of twenty THBT derivatives (in cyan) used in pharmacophore modeling. Notice the alignment of common chemical features shown in the active site. RMSDs of the benzothiophene scaffold between AX20017 and THBT derivatives were in the range of 0.615 and 1.254 Å. (B) The starting merged pharmacophore that was created from specific binding modes for AX20017 and compound SR_A6. Yellow circle for hydrophobic interaction, red arrow for the hydrogen-bond acceptor, and green arrow for the hydrogen-bond donor. RMSD of the tetrahydrobenzothiophene scaffold between SR_A6 and AX20017 was 0.735 Å.

Journal: ACS Omega

Article Title: Identifying RO9021 as a Potential Inhibitor of PknG from Mycobacterium tuberculosis : Combinative Computational and In Vitro Studies

doi: 10.1021/acsomega.2c02093

Figure Lengend Snippet: Binding modes of inhibitor AX20017 and THBT derivatives. (A) X-ray reference structure of AX20017 (in gray) (PDB ID: 2PZI ) and docked conformations of twenty THBT derivatives (in cyan) used in pharmacophore modeling. Notice the alignment of common chemical features shown in the active site. RMSDs of the benzothiophene scaffold between AX20017 and THBT derivatives were in the range of 0.615 and 1.254 Å. (B) The starting merged pharmacophore that was created from specific binding modes for AX20017 and compound SR_A6. Yellow circle for hydrophobic interaction, red arrow for the hydrogen-bond acceptor, and green arrow for the hydrogen-bond donor. RMSD of the tetrahydrobenzothiophene scaffold between SR_A6 and AX20017 was 0.735 Å.

Article Snippet: Compound AX20017 was received from the MedChem Express Library (MCE; Monmouth Junction, NJ); and the CHEMBL compounds were received from Chemspace US Inc. (Chemspace; Monmouth Junction, NJ 08852).

Techniques: Binding Assay

Pharmacophore models created using the structured-based approach of LigandScout. (A) Pharmacophore model for PknG-AX20017 (PDB: 2PZI ) using parameters by default. (B) Pharmacophore model for PknG-AX20017 with excluded volumes (gray spheres) added by default. (C) Initial pharmacophore model for PknG by the merged approach. Pharmacophore models for compounds AX20017 and SR_A6 were aligned and then merged using the alignment module of LigandScout. The merged pharmacophore is composed of three hydrophobic features, two hydrogen-bond donor features, and two hydrogen-bond acceptor features. (D) Optimized pharmacophore model for PknG with excluded volumes (gray spheres) manually added to avoid inactive molecules. Yellow circle for hydrophobic interaction, red arrow for the hydrogen-bond acceptor, and green arrow for the hydrogen-bond donor.

Journal: ACS Omega

Article Title: Identifying RO9021 as a Potential Inhibitor of PknG from Mycobacterium tuberculosis : Combinative Computational and In Vitro Studies

doi: 10.1021/acsomega.2c02093

Figure Lengend Snippet: Pharmacophore models created using the structured-based approach of LigandScout. (A) Pharmacophore model for PknG-AX20017 (PDB: 2PZI ) using parameters by default. (B) Pharmacophore model for PknG-AX20017 with excluded volumes (gray spheres) added by default. (C) Initial pharmacophore model for PknG by the merged approach. Pharmacophore models for compounds AX20017 and SR_A6 were aligned and then merged using the alignment module of LigandScout. The merged pharmacophore is composed of three hydrophobic features, two hydrogen-bond donor features, and two hydrogen-bond acceptor features. (D) Optimized pharmacophore model for PknG with excluded volumes (gray spheres) manually added to avoid inactive molecules. Yellow circle for hydrophobic interaction, red arrow for the hydrogen-bond acceptor, and green arrow for the hydrogen-bond donor.

Article Snippet: Compound AX20017 was received from the MedChem Express Library (MCE; Monmouth Junction, NJ); and the CHEMBL compounds were received from Chemspace US Inc. (Chemspace; Monmouth Junction, NJ 08852).

Techniques:

Screening of selected candidates against kinase activity. (A) Inhibitory percentage values reported for AX20017 and selected candidates from the CHEMBL database. Initial screenings were performed with 10 μM compounds. The dashed line represents the maximum inhibitory percentage reached by AX20017 under our experimental conditions (B) Dose–response assay. The luminescence signal was normalized by subtracting the BAC signal and then calculating a ratio against the NIC reaction. (C) Dose–response assay for AX20017. The luminescence signal was plotted against the log compound concentration. Compounds were tested ranging from 100 nM to 100 μM. (D) As in (C), for RO9021.

Journal: ACS Omega

Article Title: Identifying RO9021 as a Potential Inhibitor of PknG from Mycobacterium tuberculosis : Combinative Computational and In Vitro Studies

doi: 10.1021/acsomega.2c02093

Figure Lengend Snippet: Screening of selected candidates against kinase activity. (A) Inhibitory percentage values reported for AX20017 and selected candidates from the CHEMBL database. Initial screenings were performed with 10 μM compounds. The dashed line represents the maximum inhibitory percentage reached by AX20017 under our experimental conditions (B) Dose–response assay. The luminescence signal was normalized by subtracting the BAC signal and then calculating a ratio against the NIC reaction. (C) Dose–response assay for AX20017. The luminescence signal was plotted against the log compound concentration. Compounds were tested ranging from 100 nM to 100 μM. (D) As in (C), for RO9021.

Article Snippet: Compound AX20017 was received from the MedChem Express Library (MCE; Monmouth Junction, NJ); and the CHEMBL compounds were received from Chemspace US Inc. (Chemspace; Monmouth Junction, NJ 08852).

Techniques: Activity Assay, Concentration Assay

Potential binding mode of compound RO9021. (A) X-ray reference structure of AX20017 (in gray) (PDB: 2PZI ) and docked conformation of RO9021 (cyan). (B) Main interactions in the PknG binding site for hit compound RO9021. Yellow circle for hydrophobic interaction, red arrow for the hydrogen-bond acceptor, blue star for the positive ionizable area, and green arrow for the hydrogen-bond donor.

Journal: ACS Omega

Article Title: Identifying RO9021 as a Potential Inhibitor of PknG from Mycobacterium tuberculosis : Combinative Computational and In Vitro Studies

doi: 10.1021/acsomega.2c02093

Figure Lengend Snippet: Potential binding mode of compound RO9021. (A) X-ray reference structure of AX20017 (in gray) (PDB: 2PZI ) and docked conformation of RO9021 (cyan). (B) Main interactions in the PknG binding site for hit compound RO9021. Yellow circle for hydrophobic interaction, red arrow for the hydrogen-bond acceptor, blue star for the positive ionizable area, and green arrow for the hydrogen-bond donor.

Article Snippet: Compound AX20017 was received from the MedChem Express Library (MCE; Monmouth Junction, NJ); and the CHEMBL compounds were received from Chemspace US Inc. (Chemspace; Monmouth Junction, NJ 08852).

Techniques: Binding Assay

RMSDs of RO9021 as compared to AX20017 during 100 ns of MD. (A) Time courses of MD simulation of PknG apo (gray) or AX20017-bound (pink). (B, C) as A for 6(4) and RO9021, respectively. Pink horizontal line shows the ligand thresholds based on the PknG-AX20017 complex simulation (RMSD average + 2 s.d.). (D) Representative binding mode of the MD (centroids) obtained for AX20017 RMSD-based clustering compared to the initial docked state, RMSD obtained 0.908 Å. (E) as (D) for compound 6(4), RMSD range between 1.968 and 5.610 Å (F) as (D) for RO9021, RMSD obtained 1.676 Å. In (D)–(F). Protein atoms are represented by transparent cartoons. Ligands are depicted as sticks and their atoms are colored by the CPK convention. The initial docked state is colored gray (D), orange (E), and cyan (F). The unique representative binding modes of AX20017 and RO9021 are colored in green RO9021. For clarity, only 3 of the 10 representative binding modes of 6(4) are shown, for a complete list see Table S4 . The binding states are colored using a grayscale where lighter grays indicate that the centroid corresponds to a time frame further along the simulation.

Journal: ACS Omega

Article Title: Identifying RO9021 as a Potential Inhibitor of PknG from Mycobacterium tuberculosis : Combinative Computational and In Vitro Studies

doi: 10.1021/acsomega.2c02093

Figure Lengend Snippet: RMSDs of RO9021 as compared to AX20017 during 100 ns of MD. (A) Time courses of MD simulation of PknG apo (gray) or AX20017-bound (pink). (B, C) as A for 6(4) and RO9021, respectively. Pink horizontal line shows the ligand thresholds based on the PknG-AX20017 complex simulation (RMSD average + 2 s.d.). (D) Representative binding mode of the MD (centroids) obtained for AX20017 RMSD-based clustering compared to the initial docked state, RMSD obtained 0.908 Å. (E) as (D) for compound 6(4), RMSD range between 1.968 and 5.610 Å (F) as (D) for RO9021, RMSD obtained 1.676 Å. In (D)–(F). Protein atoms are represented by transparent cartoons. Ligands are depicted as sticks and their atoms are colored by the CPK convention. The initial docked state is colored gray (D), orange (E), and cyan (F). The unique representative binding modes of AX20017 and RO9021 are colored in green RO9021. For clarity, only 3 of the 10 representative binding modes of 6(4) are shown, for a complete list see Table S4 . The binding states are colored using a grayscale where lighter grays indicate that the centroid corresponds to a time frame further along the simulation.

Article Snippet: Compound AX20017 was received from the MedChem Express Library (MCE; Monmouth Junction, NJ); and the CHEMBL compounds were received from Chemspace US Inc. (Chemspace; Monmouth Junction, NJ 08852).

Techniques: Binding Assay

Protein RMSF and ligand interaction mapping from PknG-AX20017 and PknG-RO9021 complexes. (A, B) Protein RMSFs of protein–ligand complexes ( holo -PknG) are given (pink lines). Protein RMSF of the apo -PknG simulation is also shown in each plot (black line) to facilitate comparison. Blue arrows indicate differences between apo- and holo- structures present in both, PknG-AX20017 and PknG-RO9021 complexes. (C, D) The frequency of different types of interactions per protein residue is expressed as a percentage of the ligand’s total interactions and shown in stacked bar plots. Residues with less than 2.5% of the ligand’s total interactions were omitted. The panels show analysis for complexes with (A/C) AX20017 and (B/D) RO9021.

Journal: ACS Omega

Article Title: Identifying RO9021 as a Potential Inhibitor of PknG from Mycobacterium tuberculosis : Combinative Computational and In Vitro Studies

doi: 10.1021/acsomega.2c02093

Figure Lengend Snippet: Protein RMSF and ligand interaction mapping from PknG-AX20017 and PknG-RO9021 complexes. (A, B) Protein RMSFs of protein–ligand complexes ( holo -PknG) are given (pink lines). Protein RMSF of the apo -PknG simulation is also shown in each plot (black line) to facilitate comparison. Blue arrows indicate differences between apo- and holo- structures present in both, PknG-AX20017 and PknG-RO9021 complexes. (C, D) The frequency of different types of interactions per protein residue is expressed as a percentage of the ligand’s total interactions and shown in stacked bar plots. Residues with less than 2.5% of the ligand’s total interactions were omitted. The panels show analysis for complexes with (A/C) AX20017 and (B/D) RO9021.

Article Snippet: Compound AX20017 was received from the MedChem Express Library (MCE; Monmouth Junction, NJ); and the CHEMBL compounds were received from Chemspace US Inc. (Chemspace; Monmouth Junction, NJ 08852).

Techniques: Comparison, Residue

Performance Parameters for Optimized Merged Pharmacophore Model (AX20017-SR_A6)

Journal: ACS Omega

Article Title: Identifying RO9021 as a Potential Inhibitor of PknG from Mycobacterium tuberculosis : Combinative Computational and In Vitro Studies

doi: 10.1021/acsomega.2c02093

Figure Lengend Snippet: Performance Parameters for Optimized Merged Pharmacophore Model (AX20017-SR_A6)

Article Snippet: Compound AX20017 was received from the MedChem Express Library (MCE; Monmouth Junction, NJ); and the CHEMBL compounds were received from Chemspace US Inc. (Chemspace; Monmouth Junction, NJ 08852).

Techniques:

Selected CHEMBL Candidates Based on the Two Sets of Criteria toward Mtb PknG

Journal: ACS Omega

Article Title: Identifying RO9021 as a Potential Inhibitor of PknG from Mycobacterium tuberculosis : Combinative Computational and In Vitro Studies

doi: 10.1021/acsomega.2c02093

Figure Lengend Snippet: Selected CHEMBL Candidates Based on the Two Sets of Criteria toward Mtb PknG

Article Snippet: Compound AX20017 was received from the MedChem Express Library (MCE; Monmouth Junction, NJ); and the CHEMBL compounds were received from Chemspace US Inc. (Chemspace; Monmouth Junction, NJ 08852).

Techniques:

Selected CHEMBL Candidates Based on Pharmacophore-Match and Pharmacophore Fit-Score toward Mtb PknG

Journal: ACS Omega

Article Title: Identifying RO9021 as a Potential Inhibitor of PknG from Mycobacterium tuberculosis : Combinative Computational and In Vitro Studies

doi: 10.1021/acsomega.2c02093

Figure Lengend Snippet: Selected CHEMBL Candidates Based on Pharmacophore-Match and Pharmacophore Fit-Score toward Mtb PknG

Article Snippet: Compound AX20017 was received from the MedChem Express Library (MCE; Monmouth Junction, NJ); and the CHEMBL compounds were received from Chemspace US Inc. (Chemspace; Monmouth Junction, NJ 08852).

Techniques: