Crimean Congo Hemorrhagic Fever Virus OTU domain in complex with ubiquitin-propargyl. Determined by X-ray diffraction at 2.3 Å resolution. Released 27 Feb 2013.
Explore 3ZNH in 3D Show helices and sheets RCSB PDB PDBe
3ZNH contains 11 α-helices and 18 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 |
|---|---|---|---|
| β-strand | 10-13 | 4 | 1 |
| β-strand | 16-19 | 4 | 1 |
| β-strand | 24 | 1 | 2 |
| α-helix | 25-27 | 3 | |
| β-strand | 29-32 | 4 | 1 |
| α-helix | 40-49 | 10 | |
| α-helix | 58-72 | 15 | |
| α-helix | 73-75 | 3 | |
| α-helix | 79-82 | 4 | |
| α-helix | 86-93 | 8 | |
| β-strand | 101 | 1 | 3 |
| α-helix | 102-111 | 10 | |
| β-strand | 116-121 | 6 | 1 |
| β-strand | 126 | 1 | 2 |
| β-strand | 127-133 | 7 | 1 |
| β-strand | 142-147 | 6 | 1 |
| β-strand | 151-157 | 7 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 2-6 | 5 | 4 |
| β-strand | 12-16 | 5 | 4 |
| β-strand | 22 | 1 | 5 |
| α-helix | 23-34 | 12 | |
| α-helix | 38-40 | 3 | |
| β-strand | 41-45 | 5 | 4 |
| β-strand | 48-49 | 2 | 4 |
| α-helix | 50-51 | 2 | |
| β-strand | 55 | 1 | 5 |
| β-strand | 66-71 | 6 | 4 |
| α-helix | 72 | 1 | |
| β-strand | 74 | 1 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ubiquitin thioesterase | A | protein | 183 | CRIMEAN-CONGO HEMORRHAGIC FEVER VIRUS | Q6TQR6 (AlphaFold model) |
| Polyubiquitin-B | B | protein | 76 | HOMO SAPIENS | P0CG47 (AlphaFold model) |
>3ZNH_1 UBIQUITIN THIOESTERASE (chains A) MDFLRSLDWTQVIAGQYVSNPRFNISDYFEIVRQPGDGNCFYHSIAELTMPNKTDHSYHY IKRLTESAARKYYQEEPEARLVGLSLEDYLKRMLSDNEWGSTLEASMLAKEMGITIIIWT VAASDEVEAGIKFGDGDVFTAVNLLHSGQTHFDALRILPQFETDTREALSLMDRVIAVDQ LTS
>3ZNH_2 POLYUBIQUITIN-B (chains B) MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYN IQKESTLHLVLRLRGX
On Terminal Alkynes that Can React with Active-Site Cysteine Nucleophiles in Proteases. Ekkebus, R., Van Kasteren, S.I., Kulathu, Y. et al. J Am Chem Soc (2013) 135:2867. DOI 10.1021/JA309802N · PubMed
Other PDB entries of the same protein (UniProt Q6TQR6 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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