Crystal Structure of PYK2-Apo, Proline-rich Tyrosine Kinase. Determined by X-ray diffraction at 2.2 Å resolution. Released 31 Mar 2009.
Explore 3FZO in 3D Show helices and sheets RCSB PDB PDBe
3FZO contains 19 α-helices and 9 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 422-424 | 3 | |
| β-strand | 425-433 | 9 | 1 |
| β-strand | 438-445 | 8 | 1 |
| α-helix | 446 | 1 | |
| β-strand | 451-458 | 8 | 1 |
| α-helix | 465-481 | 17 | |
| β-strand | 486 | 1 | 2 |
| α-helix | 487-488 | 2 | |
| β-strand | 489-493 | 5 | 1 |
| β-strand | 499-503 | 5 | 1 |
| β-strand | 509 | 1 | 2 |
| α-helix | 510-517 | 8 | |
| α-helix | 523-542 | 20 | |
| α-helix | 552-554 | 3 | |
| β-strand | 555-559 | 5 | 2 |
| β-strand | 562-565 | 4 | 2 |
| α-helix | 567-569 | 3 | |
| α-helix | 570-573 | 4 | |
| α-helix | 589-591 | 3 | |
| α-helix | 594-599 | 6 | |
| α-helix | 604-619 | 16 | |
| α-helix | 623-624 | 2 | |
| α-helix | 631-639 | 9 | |
| α-helix | 644-647 | 4 | |
| α-helix | 652-661 | 10 | |
| α-helix | 666-668 | 3 | |
| α-helix | 670-671 | 2 | |
| α-helix | 672-689 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein tyrosine kinase 2 beta | A | protein | 277 | Homo sapiens | Q14289 (AlphaFold model) |
>3FZO_1 Protein tyrosine kinase 2 beta (chains A) PQYGIAREDVVLNRILGEGFFGEVYEGVYTNHKGEKINVAVKTCKKDCTLDNKEKFMSEA VIMKNLDHPHIVKLIGIIEEEPTWIIMELYPYGELGHYLERNKNSLKVLTLVLYSLQICK AMAYLESINCVHRDIAVRNILVASPECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPE SINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEKGDRLPKPDLCPPVLY TLMTRCWDYDPSDRPRFTELVCSLSDVYQMEKDIAME
Structural characterization of proline-rich tyrosine kinase 2 (PYK2) reveals a unique (DFG-out) conformation and enables inhibitor design. Han, S., Mistry, A., Chang, J.S. et al. J Biol Chem (2009) 284:13193-13201. DOI 10.1074/jbc.M809038200 · PubMed
Other PDB entries of the same protein (UniProt Q14289 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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