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
- 6LXF
- Type
- protein
- Length
- 57 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polyprotein
- UniProt
- Q9EB08
Structure
solution nmr · 1 distinct chain · 11% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Polyprotein | protein | 57 | 11% helix, 28% strand | Q9EB08 |
Compared structures
- 6LXF · Aromatic interactions drive the coupled folding and binding of the intrinsically… · the same entry in another collection · chain B against B, 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 6LXF · PDBe 6LXF · UniProt Q9EB08
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