Research workbench
Aromatic interactions drive the coupled folding and binding of the intrinsically disordered sesbania mosaic virus vpg protein
Analyse Aromatic interactions drive the coupled folding and binding of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6M78
- Type
- protein
- Length
- 248 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polyprotein
- UniProt
- Q9EB08
- Pockets
- 2 · best druggability 0.46
Structure
solution nmr · 2 distinct chains · 8% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Polyprotein | protein | 191 | 8% helix, 43% strand | Q9EB08 |
| B | Polyprotein | protein | 57 | 7% helix, 21% strand | Q9EB08 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 113 | 0.46 | 0.78 | 22 | empty |
| 2 | 80 | 0.32 | 0.74 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 727 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6M78 · Aromatic interactions drive the coupled folding and binding of the intrinsically… · 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 Q9EB08
- Elsewhere: RCSB PDB 6M78 · PDBe 6M78 · UniProt Q9EB08
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