Crystal structure of human Wee1 kinase domain in complex with inhibitor. Determined by X-ray diffraction at 1.96 Å resolution. Released 10 Sept 2025.
Explore 9D0Q in 3D Show helices and sheets RCSB PDB PDBe
9D0Q contains 33 α-helices and 22 β-strands across 2 chains. 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 | 294-298 | 5 | |
| β-strand | 299-308 | 10 | 1 |
| β-strand | 311-318 | 8 | 1 |
| β-strand | 324-331 | 8 | 1 |
| α-helix | 332-334 | 3 | |
| α-helix | 338-353 | 16 | |
| β-strand | 359 | 1 | 2 |
| β-strand | 362-368 | 7 | 1 |
| β-strand | 371-377 | 7 | 1 |
| β-strand | 383 | 1 | 2 |
| α-helix | 384-393 | 10 | |
| α-helix | 400-419 | 20 | |
| β-strand | 422-423 | 2 | 3 |
| α-helix | 429-431 | 3 | |
| β-strand | 432-436 | 5 | 2 |
| β-strand | 457-461 | 5 | 2 |
| α-helix | 464-466 | 3 | |
| β-strand | 468-469 | 2 | 3 |
| α-helix | 485-488 | 4 | |
| α-helix | 495-510 | 16 | |
| α-helix | 521-527 | 7 | |
| α-helix | 530-533 | 4 | |
| α-helix | 540-549 | 10 | |
| α-helix | 554-556 | 3 | |
| α-helix | 558-559 | 2 | |
| α-helix | 560-564 | 5 | |
| α-helix | 567-570 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 294-298 | 5 | |
| β-strand | 299-307 | 9 | 4 |
| β-strand | 311-318 | 8 | 4 |
| β-strand | 324-331 | 8 | 4 |
| α-helix | 332-334 | 3 | |
| α-helix | 338-353 | 16 | |
| β-strand | 359 | 1 | 5 |
| β-strand | 362-368 | 7 | 4 |
| β-strand | 371-377 | 7 | 4 |
| β-strand | 383 | 1 | 5 |
| α-helix | 384-394 | 11 | |
| α-helix | 400-419 | 20 | |
| β-strand | 422-423 | 2 | 6 |
| α-helix | 429-431 | 3 | |
| β-strand | 432-437 | 6 | 5 |
| β-strand | 456-461 | 6 | 5 |
| α-helix | 464-466 | 3 | |
| β-strand | 468-469 | 2 | 6 |
| α-helix | 480-482 | 3 | |
| α-helix | 485-488 | 4 | |
| α-helix | 495-510 | 16 | |
| α-helix | 521-527 | 7 | |
| α-helix | 530-533 | 4 | |
| α-helix | 540-549 | 10 | |
| α-helix | 554-556 | 3 | |
| α-helix | 558-559 | 2 | |
| α-helix | 560-564 | 5 | |
| α-helix | 567-572 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Wee1-like protein kinase | A, B | protein | 289 | Homo sapiens | P30291 (AlphaFold model) |
>9D0Q_1 Wee1-like protein kinase (chains A, B) GAMGMKSRYTTEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALRE VYAHAVLGQHSHVVRYFSAWAEDDHMLIQNEYCNGGSLADAISENYRIMSYFKEAELKDL LLQVGRGLRYIHSMSLVHMDIKPSNIFISRTSIPNAASEEGDEDDWASNKVMFKIGDLGH VTRISSPQVEEGDSRFLANEVLQENYTHLPKADIFALALTVVCAAGAEPLPRNGDQWHEI RQGRLPRIPQVLSQEFTELLKVMIHPDPERRPSAMALVKHSVLLSASRK
| ID | Name | Formula | Copies |
|---|---|---|---|
| A1A1S | 1-[(6R)-6-(2,6-dichlorophenyl)-8-methyl-2-[4-(4-methylpiperazin-1-yl)anilino]-7… | C26 H29 Cl2 N7 O | 2 |
Water and common crystallization additives (CL, NA) are not listed.
Harnessing free energy calculations for kinome-wide selectivity in drug discovery campaigns with a Wee1 case study. Knight, J.L., Clark, A.J., Wang, J. et al. Nat Commun (2025) 16:7962-7962. DOI 10.1038/s41467-025-62722-w · PubMed
Other PDB entries of the same protein (UniProt P30291 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 9D0Q directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.