Research workbench
Crystal structure of bacteriophage MS2 covalent coat protein dimer
Analyse Crystal structure of bacteriophage MS2 covalent coat protein dimer in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VTU
- Type
- protein
- Length
- 514 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MS2 coat protein
- UniProt
- P03612
- Pockets
- 8 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 13% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| J, L | MS2 coat protein | protein | 257 | 13% helix, 16% strand | P03612 |
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 177 | 0.52 | 0.78 | 31 | empty |
| 2 | 157 | 0.47 | 0.76 | 22 | empty |
| 3 | 137 | 0.43 | 0.76 | 26 | empty |
| 4 | 124 | 0.42 | 0.76 | 23 | empty |
| 5 | 97 | 0.42 | 0.78 | 23 | empty |
Interfaces
1 interface between chains.
- J–L · 1957 Ų buried · 28 hydrogen bonds · protein-protein
Compared structures
- 2VTU · crystal structure of bacteriophage MS2 covalent coat protein dimer · the same entry in another collection · chain J against J, 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 2VTU · PDBe 2VTU · UniProt P03612
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.