EPHB2 (EphB2)

EPH receptor B2
Group TK Family Eph Species Human UniProt P29323 IUPHAR/BPS 1831 All structures in KLIFS search
1
structures
1 PDB entries
0
unique orthosteric ligands
0 ligand-bound, 1 apo
2.27
best resolution (Å)
 
2014
first structure
latest: 2014-01-08
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.
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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
PDBChainAlt.LigandHet IDBinding modeDFGαCRes. (Å)QualityReleasedMissing res.View