MolNFT v1 · #156233 · protein
Aromatic interactions drive the coupled folding and binding of the intrinsically disordered sesbania mosaic virus vpg protein.
6LXF · Polyprotein: “Aromatic interactions drive the coupled folding and binding of the intrinsically disordered sesbania mosaic…”. Solution nmr. MolNFT v1 #156233 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- 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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