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-Structure paper
Title | Structural characterization of proline-rich tyrosine kinase 2 (PYK2) reveals a unique (DFG-out) conformation and enables inhibitor design. |
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Journal, issue, pages | J. Biol. Chem., Vol. 284, Page 13193-13201, Year 2009 |
Publish date | Jan 26, 2009 (structure data deposition date) |
![]() | Han, S. / Mistry, A. / Chang, J.S. / Cunningham, D. / Griffor, M. / Bonnette, P.C. / Wang, H. / Chrunyk, B.A. / Aspnes, G.E. / Walker, D.P. ...Han, S. / Mistry, A. / Chang, J.S. / Cunningham, D. / Griffor, M. / Bonnette, P.C. / Wang, H. / Chrunyk, B.A. / Aspnes, G.E. / Walker, D.P. / Brosius, A.D. / Buckbinder, L. |
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Methods | X-ray diffraction |
Resolution | 1.75 - 2.7 Å |
Structure data | ![]() PDB-3fzo: ![]() PDB-3fzp: ![]() PDB-3fzr: ![]() PDB-3fzs: ![]() PDB-3fzt: |
Chemicals | ![]() ChemComp-HOH: ![]() ChemComp-AGS: ![]() ChemComp-SO4: ![]() ChemComp-3JZ: ![]() ChemComp-PO4: ![]() ChemComp-B96: ![]() ChemComp-4JZ: |
Source |
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![]() | TRANSFERASE / tyrosine kinase / dfg-out / Alternative splicing / ATP-binding / Cell membrane / Cytoplasm / Kinase / Membrane / Nucleotide-binding / Phosphoprotein / Polymorphism / Tyrosine-protein kinase / ATPgS / DFG / PYK2 |