OTU Domain of Crimean Congo Hemorrhagic Fever Virus in complex with ISG15. Determined by X-ray diffraction at 1.6 Å resolution. Released 2 Feb 2011.
Explore 3PHX in 3D Show helices and sheets RCSB PDB PDBe
3PHX contains 13 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 |
|---|---|---|---|
| α-helix | 3-6 | 4 | |
| β-strand | 10-13 | 4 | 1 |
| β-strand | 16-19 | 4 | 1 |
| β-strand | 24 | 1 | 2 |
| α-helix | 25-28 | 4 | |
| 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 | 102-112 | 11 | |
| β-strand | 116-120 | 5 | 1 |
| β-strand | 126 | 1 | 2 |
| β-strand | 129-133 | 5 | 1 |
| β-strand | 142-147 | 6 | 1 |
| β-strand | 151-157 | 7 | 1 |
| α-helix | 159-161 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 82-87 | 6 | 4 |
| β-strand | 93-98 | 6 | 4 |
| β-strand | 103 | 1 | 5 |
| α-helix | 104-115 | 12 | |
| α-helix | 119-121 | 3 | |
| β-strand | 122-126 | 5 | 4 |
| β-strand | 129-130 | 2 | 4 |
| α-helix | 131-132 | 2 | |
| β-strand | 136 | 1 | 5 |
| α-helix | 137-140 | 4 | |
| β-strand | 147-152 | 6 | 4 |
| β-strand | 155 | 1 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RNA-directed RNA polymerase L | A | protein | 185 | Crimean-Congo hemorrhagic fever virus | Q6TQR6 (AlphaFold model) |
| Ubiquitin-like protein ISG15 | B | protein | 79 | Homo sapiens | P05161 (AlphaFold model) |
>3PHX_1 RNA-directed RNA polymerase L (chains A) GPMDFLRSLDWTQVIAGQYVSNPRFNISDYFEIVRQPGDGNCFYHSIAELTMPNKTDHSY HYIKRLTESAARKYYQEEPEARLVGLSLEDYLKRMLSDNEWGSTLEASMLAKEMGITIII WTVAASDEVEAGIKFGDGDVFTAVNLLHSGQTHFDALRILPQFETDTREALSLMDRVIAV DQLTS
>3PHX_2 Ubiquitin-like protein ISG15 (chains B) MDEPLSILVRNNKGRSSTYEVRLTQTVAHLKQQVSGLEGVQDDLFWLTFEGKPLEDQLPL GEYGLKPLSTVFMNLRLRG
Water and common crystallization additives (ACY) are not listed.
Molecular basis for ubiquitin and ISG15 cross-reactivity in viral ovarian tumor domains. Akutsu, M., Ye, Y., Virdee, S. et al. Proc Natl Acad Sci U S A (2011) 108:2228-2233. DOI 10.1073/pnas.1015287108 · 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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