Crystal structure of USP16 ZnF-UBP domain. Determined by X-ray diffraction at 1.8 Å resolution. Released 20 May 2026.
Explore 9YCW in 3D Show helices and sheets RCSB PDB PDBe
9YCW contains 16 α-helices and 15 β-strands across 3 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 | 10-14 | 5 | |
| α-helix | 19-22 | 4 | |
| β-strand | 54-57 | 4 | 1 |
| β-strand | 63-65 | 3 | 1 |
| α-helix | 73-79 | 7 | |
| β-strand | 88-91 | 4 | 1 |
| β-strand | 97-99 | 3 | 1 |
| β-strand | 104-106 | 3 | 1 |
| α-helix | 107 | 1 | |
| α-helix | 113-125 | 13 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-14 | 5 | |
| α-helix | 19-22 | 4 | |
| α-helix | 26-27 | 2 | |
| α-helix | 32-35 | 4 | |
| β-strand | 54-57 | 4 | 2 |
| β-strand | 63-65 | 3 | 2 |
| α-helix | 73-79 | 7 | |
| β-strand | 88-91 | 4 | 2 |
| β-strand | 97-99 | 3 | 2 |
| β-strand | 104-106 | 3 | 2 |
| α-helix | 113-126 | 14 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 10-14 | 5 | |
| α-helix | 19-22 | 4 | |
| β-strand | 54-57 | 4 | 3 |
| β-strand | 63-65 | 3 | 3 |
| α-helix | 73-79 | 7 | |
| β-strand | 88-91 | 4 | 3 |
| β-strand | 97-99 | 3 | 3 |
| β-strand | 104-106 | 3 | 3 |
| α-helix | 107 | 1 | |
| α-helix | 113-124 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin carboxyl-terminal hydrolase 16 | A, B, C | protein | 125 | Homo sapiens | Q9Y5T5 (AlphaFold model) |
>9YCW_1 Ubiquitin carboxyl-terminal hydrolase 16 (chains A, B, C) GPPVCRHIRKGLEQGNLKKALVNVEWNICQDCKTDNKVKDKAEEETEEKPSVWLCLKCGH QGCGRNSQEQHALKHYLTPRSEPHCLVLSLDNWSVWCYVCDNEVQYCSSNQLGQVVDYVR KQASI
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 9 |
Water and common crystallization additives (GOL) are not listed.
The ZnF-UBP domain regulates USP16 activity by dislodging ubiquitin from the active site. Alexandrovics, J.A., Agrata, R., Schenk, P. et al. To be published.
Other PDB entries of the same protein (UniProt Q9Y5T5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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