Research workbench
Lebetin peptides, a new class of potent aggregation inhibitors
Analyse Lebetin peptides, a new class of potent aggregation inhibitors in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Q01
- Type
- protein
- Length
- 38 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Lebetin 2 isoform alpha
- UniProt
- Q7LZ09
Structure
solution nmr · 1 distinct chain · 0% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lebetin 2 isoform alpha | protein | 38 | 0% helix, 0% strand | Q7LZ09 |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
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 Q7LZ09
- Elsewhere: RCSB PDB 1Q01 · PDBe 1Q01 · UniProt Q7LZ09
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