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Bluetongue virus structure reveals a sialic acid binding domain, amphipathic helices and a central coiled coil in the outer capsid proteins
Analyse Bluetongue virus structure reveals a sialic acid binding domain, amphipathic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3IYK
- Type
- protein
- Length
- 2,265 residues
- Chains
- 9
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- VP5; VP2
- UniProt
- C5IWW1, C5IWV8
- Ligands
- MNA
Structure
electron microscopy · 2 distinct chains · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | VP5 | protein | 307 | 0% helix, 0% strand | C5IWW1 |
| G, I, K | VP2 | protein | 141 | 0% helix, 0% strand | C5IWV8 |
Ligands and binding sites
- MNA · 2-O-methyl-5-N-acetyl-alpha-D-neuraminic acid · ligand · 3 copies · chains G, I, K
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
10 interfaces between chains.
- B–C · 162 Ų buried · 0 hydrogen bonds · protein-protein
- E–F · 161 Ų buried · 0 hydrogen bonds · protein-protein
- D–E · 152 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 151 Ų buried · 0 hydrogen bonds · protein-protein
- D–F · 145 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3IYK · Bluetongue virus structure reveals a sialic acid binding domain, amphipathic helices and… · the same entry in another collection · chain A against A, TM-score 1.00
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 C5IWW1
- Every structure of UniProt C5IWV8
- Elsewhere: RCSB PDB 3IYK · PDBe 3IYK · UniProt C5IWW1 · UniProt C5IWV8
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