The ubiquitin-associated domain of human thirty-eight negative kinase-1 rigidly fused to a double trigger variant of the 1TEL crystallization chaperone, alternate crystal form. Determined by X-ray diffraction at 1.96 Å resolution. Released 4 Mar 2026.
Explore 9ZVU in 3D Show helices and sheets RCSB PDB PDBe
9ZVU contains 23 α-helices and 0 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 | 24-26 | 3 | |
| α-helix | 29-42 | 14 | |
| α-helix | 45-47 | 3 | |
| α-helix | 50-53 | 4 | |
| α-helix | 57-61 | 5 | |
| α-helix | 65-71 | 7 | |
| α-helix | 76-100 | 25 | |
| α-helix | 106-115 | 10 | |
| α-helix | 120-133 | 14 | |
| α-helix | 140-149 | 10 | |
| α-helix | 154-163 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 15-17 | 3 | |
| α-helix | 18-21 | 4 | |
| α-helix | 24-26 | 3 | |
| α-helix | 29-43 | 15 | |
| α-helix | 45-47 | 3 | |
| α-helix | 57-60 | 4 | |
| α-helix | 65-71 | 7 | |
| α-helix | 76-100 | 25 | |
| α-helix | 106-115 | 10 | |
| α-helix | 120-133 | 14 | |
| α-helix | 140-149 | 10 | |
| α-helix | 154-163 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transcription factor ETV6,Non-receptor tyrosine-protein kinase TNK1 | A, B | protein | 165 | Homo sapiens | P41212 (AlphaFold model), Q13470 (AlphaFold model) |
>9ZVU_1 Transcription factor ETV6,Non-receptor tyrosine-protein kinase TNK1 (chains A, B) MGHHHHHHHHHHSIRLPAHLRLQPIYWSRDDVAQWLKWAENEFSLSPIDSNTFEMNGKAL LELTKEDFRYRSPHSGDELYELLQHILKEVQRKIMEVELSVHGVTHQEAQTALGATGGDV VSAIRNLKVDQLFHLSSRSRADAWRILEHYQWDLSAASRYVLARP
Water and common crystallization additives (SO4, NA) are not listed.
Modulating the pH sensitivity of the TELSAM crystallization chaperone for increased solubility. Averett, J.C., Moody, J.D. 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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