Research workbench
T=3 MS2 virus-like particle
Analyse T=3 MS2 virus-like particle in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6RRS
- Type
- protein
- Length
- 387 residues
- Chains
- 3
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid protein
- UniProt
- P03612
- Pockets
- 1 · best druggability 0.24
Structure
electron microscopy · 1 distinct chain · 18% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Capsid protein | protein | 129 | 18% helix, 46% strand | P03612 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 60 | 0.24 | 0.71 | 21 | empty |
Interfaces
3 interfaces between chains.
- A–C · 185 Ų buried · 3 hydrogen bonds · protein-protein
- B–C · 176 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 161 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6RRS · T=3 MS2 Virus-like particle · 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 P03612
- Elsewhere: RCSB PDB 6RRS · PDBe 6RRS · UniProt P03612
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