TNK2 (ACK)
tyrosine kinase, non-receptor, 2
32
structures
14 PDB entries
11
unique orthosteric ligands
22 ligand-bound, 10 apo
1.31
best resolution (Å)
2004
first structure
latest: 2023-12-13
DFG conformation
αC-helix
Inhibitor binding mode ?
How is the binding mode derived?
KLIFS annotates the DFG/αC conformation and which (sub)pockets a ligand occupies; it does not store the inhibitor type. The mode shown here is derived from those annotations, so treat it as an approximation: Type I: DFG-in, ligand in the ATP site, back pocket empty; Type I½: DFG-in with back pocket occupied; Type II: DFG-out with back pocket occupied; Type III: back pocket occupied, front pocket empty; Allosteric: only an allosteric ligand outside the main pocket; Other: ligand-bound structures that fit none of these (e.g. DFG-out-like or αC/DFG not assigned); Apo: no ligand.
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3D structure
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Kinase colored by interaction frequency at the 85 pocket positions; spheres and sticks mark the top hotspots. Click a table row's eye to change structure.
Kinase fold click a residue to search
Interaction overview 85 pocket positions × interaction types — click a cell to filter the structures below, shift-click to require no interaction
Targeted (sub)pockets number of ligand-bound structures occupying each pocket
Structures
| PDB | Chain | Alt. | Ligand | Het ID | Binding mode | DFG | αC | Res. (Å) | Quality | Released | Missing res. | View |
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