Research workbench
Crystal structure of the borna disease virus matrix protein (bdv-M) reveals RNA binding properties
Analyse Crystal structure of the borna disease virus matrix protein (bdv-M) reveals RNA… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F1J
- Type
- protein
- Length
- 140 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Matrix protein
- UniProt
- P52637
- Ligands
- C5P, SO4
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 23% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Matrix protein | protein | 140 | 23% helix, 32% strand | P52637 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 52 | 0.35 | 0.79 | 13 | empty |
Modifications
Observed in the structure: 2 modified (engineered).
Compared structures
- 3F1J · Crystal structure of the Borna disease virus matrix protein (BDV-M) reveals RNA binding… · 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 P52637
- Elsewhere: RCSB PDB 3F1J · PDBe 3F1J · UniProt P52637
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.