Research workbench
T=4 MS2 virus-like-particle
Analyse T=4 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
- 6RRT
- Type
- protein
- Length
- 512 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Capsid protein
- UniProt
- P03612
- Pockets
- 2 · best druggability 0.68
Structure
electron microscopy · 1 distinct chain · 18% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Capsid protein | protein | 128 | 18% helix, 46% strand | P03612 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 804 | 0.68 | 0.76 | 116 | empty |
| 2 | 371 | 0.57 | 0.76 | 56 | empty |
Interfaces
5 interfaces between chains.
- C–D · 705 Ų buried · 17 hydrogen bonds · protein-protein
- B–D · 180 Ų buried · 3 hydrogen bonds · protein-protein
- A–B · 160 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 153 Ų buried · 3 hydrogen bonds · protein-protein
- A–D · 144 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 6RRT · T=4 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 6RRT · PDBe 6RRT · UniProt P03612
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