Structure of the PYK2 from Biortus. Determined by X-ray diffraction at 2.0 Å resolution. Released 13 Mar 2024.
Explore 8YGX in 3D Show helices and sheets RCSB PDB PDBe
8YGX contains 18 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 |
| β-strand | 451-457 | 7 | 1 |
| α-helix | 465-481 | 17 | |
| β-strand | 486 | 1 | 2 |
| α-helix | 487-488 | 2 | |
| β-strand | 489-493 | 5 | 1 |
| α-helix | 498 | 1 | |
| β-strand | 499-503 | 5 | 1 |
| α-helix | 504-505 | 2 | |
| β-strand | 509 | 1 | 2 |
| α-helix | 510-516 | 7 | |
| α-helix | 523-542 | 20 | |
| α-helix | 552-554 | 3 | |
| β-strand | 555-559 | 5 | 2 |
| β-strand | 562-565 | 4 | 2 |
| α-helix | 589-591 | 3 | |
| α-helix | 594-599 | 6 | |
| α-helix | 604-619 | 16 | |
| α-helix | 623-624 | 2 | |
| α-helix | 631-640 | 10 | |
| α-helix | 644-647 | 4 | |
| α-helix | 652-661 | 10 | |
| α-helix | 666-668 | 3 | |
| α-helix | 670-671 | 2 | |
| α-helix | 672-690 | 19 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein-tyrosine kinase 2-beta | A | protein | 277 | Homo sapiens | Q14289 (AlphaFold model) |
>8YGX_1 Protein-tyrosine kinase 2-beta (chains A) PQYGIAREDVVLNRILGEGFFGEVYEGVYTNHKGEKINVAVKTCKKDCTLDNKEKFMSEA VIMKNLDHPHIVKLIGIIEEEPTWIIMELYPYGELGHYLERNKNSLKVLTLVLYSLQICK AMAYLESINCVHRDIAVRNILVASPECVKLGDFGLSRYIEDEDYYKASVTRLPIKWMSPE SINFRRFTTASDVWMFAVCMWEILSFGKQPFFWLENKDVIGVLEKGDRLPKPDLCPPVLY TLMTRCWDYDPSDRPRFTELVCSLSDVYQMEKDIAME
Structure of the PYK2 from Biortus. Wang, F., Cheng, W., Lv, Z. et al. To be published.
Other PDB entries of the same protein (UniProt Q14289 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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