The ubiquitin-associated domain of human thirty-eight negative kinase 1, fused to the 3TEL crystallization chaperone via a 2-glycine linker. Determined by X-ray diffraction at 2.24 Å resolution. Released 30 Apr 2025.
Explore 9O0H in 3D Show helices and sheets RCSB PDB PDBe
9O0H contains 28 α-helices and 0 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 | 7-10 | 4 | |
| α-helix | 13-15 | 3 | |
| α-helix | 18-32 | 15 | |
| α-helix | 34-36 | 3 | |
| α-helix | 39-41 | 3 | |
| α-helix | 46-49 | 4 | |
| α-helix | 54-60 | 7 | |
| α-helix | 65-78 | 14 | |
| α-helix | 92-94 | 3 | |
| α-helix | 98-100 | 3 | |
| α-helix | 103-117 | 15 | |
| α-helix | 119-121 | 3 | |
| α-helix | 124-127 | 4 | |
| α-helix | 131-134 | 4 | |
| α-helix | 139-145 | 7 | |
| α-helix | 150-163 | 14 | |
| α-helix | 183-185 | 3 | |
| α-helix | 188-202 | 15 | |
| α-helix | 204-206 | 3 | |
| α-helix | 209-211 | 3 | |
| α-helix | 216-221 | 6 | |
| α-helix | 224-230 | 7 | |
| α-helix | 235-244 | 10 | |
| α-helix | 248-258 | 11 | |
| α-helix | 266-275 | 10 | |
| α-helix | 280-295 | 16 | |
| α-helix | 300-309 | 10 | |
| α-helix | 314-321 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcription factor ETV6,Non-receptor tyrosine-protein kinase TNK1 | B | protein | 325 | Homo sapiens | P41212 (AlphaFold model), Q13470 (AlphaFold model) |
>9O0H_1 Transcription factor ETV6,Non-receptor tyrosine-protein kinase TNK1 (chains B) GSIRLPAHLRLQPIYWSRDDVAQWLKWAENEFSLRPIDSNTFEMNGKALLLLTKEDFRYR SPHSGDELYELLQHILKQRPGGGGSTSIRLPAHLRLQPIYWSRDDVAQWLKWAENEFSLR PIDSNTFEMNGKALLLLTKEDFRYRSPHSGDVLYELLQHILKQRPGGGGSTSIRLPAHLR LQPIYWSRDDVAQWLKWAENEFSLRPIDSNTFEMNGKALLLLTKEDFRYRSPHSGDVLYE LLQHILGGELQRKIMEVELSVHGVTHQEAQTALGATGGDVVSAIRNLKVDQLFHLSSRSR ADAWRILEHYQWDLSAASRYVLARP
1TEL Fusions Outperform 2TEL and 3TEL Fusions in Controlled Comparisons. Samarawickrama, P., Ludlow, K., Probst, R. et al. To be published.
Other PDB entries of the same protein (UniProt P41212 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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