Research workbench
The molecular mechanisms by which NS1 of the 1918 spanish influenza a virus hijack host protein-protein interactions
Analyse The molecular mechanisms by which NS1 of the 1918 spanish influenza a virus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ATV
- Type
- protein
- Length
- 71 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Adapter molecule crk; Proline-rich motif in iav-NS1
- UniProt
- P46108
- Ligands
- ACE, NH2
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Adapter molecule crk | protein | 58 | 5% helix, 47% strand | P46108 |
| M | Proline-rich motif in iav-NS1 | protein | 13 | 0% helix, 0% strand | — |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–M · 593 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 6ATV · The molecular mechanisms by which NS1 of the 1918 Spanish influenza A virus hijack host… · the same entry in another collection · chain A against A, TM-score 1.00
- P46108 · AlphaFold monomer V2.0 prediction for adapter molecule crk (P46108) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 P46108
- Elsewhere: RCSB PDB 6ATV · PDBe 6ATV · UniProt P46108
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