Research workbench
Otu domain of crimean congo hemorrhagic fever virus in complex with ISG15
Analyse Otu domain of crimean congo hemorrhagic fever virus in complex with ISG15 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3PHX
- Type
- protein
- Length
- 239 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA-directed RNA polymerase L; Ubiquitin-like protein ISG15
- EC
- 3.4.19.12, 2.7.7.48
- UniProt
- Q6TQR6, P05161
- Ligands
- NEH, ZN
- Pockets
- 2 · best druggability 0.46
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA-directed RNA polymerase L (EC 3.4.19.12, 2.7.7.48) | protein | 162 | 38% helix, 23% strand | Q6TQR6 |
| B | Ubiquitin-like protein ISG15 | protein | 77 | 25% helix, 36% strand | P05161 |
Ligands and binding sites
- NEH · Ethanamine · ligand · chains A, B
- ZN · Zinc ion · metal · 12 copies · chains A, B
- ACY · Acetic acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 140 | 0.46 | 0.77 | 21 | empty |
| 2 | 64 | 0.43 | 0.82 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1054 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
- 3PHX · OTU Domain of Crimean Congo Hemorrhagic Fever Virus in complex with ISG15 · the same entry in another collection · chain A against A, TM-score 1.00
- P05161 · AlphaFold monomer V2.0 prediction for ubiquitin-like protein ISG15 (P05161) · a predicted model of the same protein · chain B against A, TM-score 0.97
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q6TQR6
- Every structure of UniProt P05161
- Elsewhere: RCSB PDB 3PHX · PDBe 3PHX · UniProt Q6TQR6 · UniProt P05161
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