Review





Similar Products

pha 793887  (Verastem Inc)
86
Verastem Inc pha 793887
Structural basis of CDK5/p25 inhibition by pyrazole-based kinase inhibitors. (A) Close-up view of the ATP-binding pocket of the CDK5/p25 complex (chain A: red; chain D: blue) with Dinaciclib (cyan) bound. Key residues Leu83 and Asp86 (pink sticks) form hydrogen bonds (orange lines, distances in Å) with the inhibitor’s heterocyclic core and substituents. The surrounding protein surface is rendered semi-transparently in pink to highlight the binding cleft. (B) Global view of the CDK5/p25–Dinaciclib complex. Chain A (CDK5) is depicted as red ribbons, chain D (p25) as blue ribbons, and the molecular surface is shown in pink to delineate the active site region. Dinaciclib (cyan) occupies the canonical ATP-binding site between the N- and C-terminal lobes, consistent with its mechanism as a competitive ATP-mimetic inhibitor. (C) Chemical structures of representative pyrazole derivatives: Dinaciclib, Milciclib, <t>PHA-793887,</t> AT7519. 3D model created using SwissDock.
Pha 793887, supplied by Verastem Inc, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/pha+793887/793887+pha/pmc13269228-3-0-18
Average 86 stars, based on 1 article reviews
pha 793887 - by Bioz Stars, 2026-10
86/100 stars
  Buy from Supplier
pha 793887  (Selleck Chemicals)
93
Selleck Chemicals pha 793887
Structural basis of CDK5/p25 inhibition by pyrazole-based kinase inhibitors. (A) Close-up view of the ATP-binding pocket of the CDK5/p25 complex (chain A: red; chain D: blue) with Dinaciclib (cyan) bound. Key residues Leu83 and Asp86 (pink sticks) form hydrogen bonds (orange lines, distances in Å) with the inhibitor’s heterocyclic core and substituents. The surrounding protein surface is rendered semi-transparently in pink to highlight the binding cleft. (B) Global view of the CDK5/p25–Dinaciclib complex. Chain A (CDK5) is depicted as red ribbons, chain D (p25) as blue ribbons, and the molecular surface is shown in pink to delineate the active site region. Dinaciclib (cyan) occupies the canonical ATP-binding site between the N- and C-terminal lobes, consistent with its mechanism as a competitive ATP-mimetic inhibitor. (C) Chemical structures of representative pyrazole derivatives: Dinaciclib, Milciclib, <t>PHA-793887,</t> AT7519. 3D model created using SwissDock.
Pha 793887, supplied by Selleck Chemicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/pha+793887/PHA-793887/pm40526635-62-4-14
Average 93 stars, based on 1 article reviews
pha 793887 - by Bioz Stars, 2026-10
93/100 stars
  Buy from Supplier
pha 793887  (MedChemExpress)
92
MedChemExpress pha 793887
Structural basis of CDK5/p25 inhibition by pyrazole-based kinase inhibitors. (A) Close-up view of the ATP-binding pocket of the CDK5/p25 complex (chain A: red; chain D: blue) with Dinaciclib (cyan) bound. Key residues Leu83 and Asp86 (pink sticks) form hydrogen bonds (orange lines, distances in Å) with the inhibitor’s heterocyclic core and substituents. The surrounding protein surface is rendered semi-transparently in pink to highlight the binding cleft. (B) Global view of the CDK5/p25–Dinaciclib complex. Chain A (CDK5) is depicted as red ribbons, chain D (p25) as blue ribbons, and the molecular surface is shown in pink to delineate the active site region. Dinaciclib (cyan) occupies the canonical ATP-binding site between the N- and C-terminal lobes, consistent with its mechanism as a competitive ATP-mimetic inhibitor. (C) Chemical structures of representative pyrazole derivatives: Dinaciclib, Milciclib, <t>PHA-793887,</t> AT7519. 3D model created using SwissDock.
Pha 793887, supplied by MedChemExpress, used in various techniques. Bioz Stars score: 92/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/pha+793887/PHA-793887/pmc12173385-52-4-26
Average 92 stars, based on 1 article reviews
pha 793887 - by Bioz Stars, 2026-10
92/100 stars
  Buy from Supplier
pha 793887 selleck cat  (Selleck Chemicals)
93
Selleck Chemicals pha 793887 selleck cat
Structural basis of CDK5/p25 inhibition by pyrazole-based kinase inhibitors. (A) Close-up view of the ATP-binding pocket of the CDK5/p25 complex (chain A: red; chain D: blue) with Dinaciclib (cyan) bound. Key residues Leu83 and Asp86 (pink sticks) form hydrogen bonds (orange lines, distances in Å) with the inhibitor’s heterocyclic core and substituents. The surrounding protein surface is rendered semi-transparently in pink to highlight the binding cleft. (B) Global view of the CDK5/p25–Dinaciclib complex. Chain A (CDK5) is depicted as red ribbons, chain D (p25) as blue ribbons, and the molecular surface is shown in pink to delineate the active site region. Dinaciclib (cyan) occupies the canonical ATP-binding site between the N- and C-terminal lobes, consistent with its mechanism as a competitive ATP-mimetic inhibitor. (C) Chemical structures of representative pyrazole derivatives: Dinaciclib, Milciclib, <t>PHA-793887,</t> AT7519. 3D model created using SwissDock.
Pha 793887 Selleck Cat, supplied by Selleck Chemicals, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/pha+793887/PHA-793887/pmc12208337__mmc2-236-190-191
Average 93 stars, based on 1 article reviews
pha 793887 selleck cat - by Bioz Stars, 2026-10
93/100 stars
  Buy from Supplier
pha-793887  (ChemPartner)
90
ChemPartner pha-793887
Structural basis of CDK5/p25 inhibition by pyrazole-based kinase inhibitors. (A) Close-up view of the ATP-binding pocket of the CDK5/p25 complex (chain A: red; chain D: blue) with Dinaciclib (cyan) bound. Key residues Leu83 and Asp86 (pink sticks) form hydrogen bonds (orange lines, distances in Å) with the inhibitor’s heterocyclic core and substituents. The surrounding protein surface is rendered semi-transparently in pink to highlight the binding cleft. (B) Global view of the CDK5/p25–Dinaciclib complex. Chain A (CDK5) is depicted as red ribbons, chain D (p25) as blue ribbons, and the molecular surface is shown in pink to delineate the active site region. Dinaciclib (cyan) occupies the canonical ATP-binding site between the N- and C-terminal lobes, consistent with its mechanism as a competitive ATP-mimetic inhibitor. (C) Chemical structures of representative pyrazole derivatives: Dinaciclib, Milciclib, <t>PHA-793887,</t> AT7519. 3D model created using SwissDock.
Pha 793887, supplied by ChemPartner, used in various techniques. Bioz Stars score: 90/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/pha+793887/pha+793887/pm39754579__jm4c01686_si_001-42-18-63
Average 90 stars, based on 1 article reviews
pha-793887 - by Bioz Stars, 2026-10
90/100 stars
  Buy from Supplier

Image Search Results


Structural basis of CDK5/p25 inhibition by pyrazole-based kinase inhibitors. (A) Close-up view of the ATP-binding pocket of the CDK5/p25 complex (chain A: red; chain D: blue) with Dinaciclib (cyan) bound. Key residues Leu83 and Asp86 (pink sticks) form hydrogen bonds (orange lines, distances in Å) with the inhibitor’s heterocyclic core and substituents. The surrounding protein surface is rendered semi-transparently in pink to highlight the binding cleft. (B) Global view of the CDK5/p25–Dinaciclib complex. Chain A (CDK5) is depicted as red ribbons, chain D (p25) as blue ribbons, and the molecular surface is shown in pink to delineate the active site region. Dinaciclib (cyan) occupies the canonical ATP-binding site between the N- and C-terminal lobes, consistent with its mechanism as a competitive ATP-mimetic inhibitor. (C) Chemical structures of representative pyrazole derivatives: Dinaciclib, Milciclib, PHA-793887, AT7519. 3D model created using SwissDock.

Journal: Frontiers in Bioengineering and Biotechnology

Article Title: A patent review of cyclin-dependent kinase 5 (CDK5) inhibitors (1999–2025)

doi: 10.3389/fbioe.2026.1843047

Figure Lengend Snippet: Structural basis of CDK5/p25 inhibition by pyrazole-based kinase inhibitors. (A) Close-up view of the ATP-binding pocket of the CDK5/p25 complex (chain A: red; chain D: blue) with Dinaciclib (cyan) bound. Key residues Leu83 and Asp86 (pink sticks) form hydrogen bonds (orange lines, distances in Å) with the inhibitor’s heterocyclic core and substituents. The surrounding protein surface is rendered semi-transparently in pink to highlight the binding cleft. (B) Global view of the CDK5/p25–Dinaciclib complex. Chain A (CDK5) is depicted as red ribbons, chain D (p25) as blue ribbons, and the molecular surface is shown in pink to delineate the active site region. Dinaciclib (cyan) occupies the canonical ATP-binding site between the N- and C-terminal lobes, consistent with its mechanism as a competitive ATP-mimetic inhibitor. (C) Chemical structures of representative pyrazole derivatives: Dinaciclib, Milciclib, PHA-793887, AT7519. 3D model created using SwissDock.

Article Snippet: PHA-793887 , Pyrazole derivative , CDK5, CDK2, CDK1 , ATP-competitive; nanomolar potency , Preclinical oncology studies ( ; Verastem, Inc., 2013; ) .

Techniques: Inhibition, Binding Assay