Research workbench
Beta-endorphin amyloid fibril
Analyse Beta-endorphin amyloid fibril in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6TUB
- Type
- protein
- Length
- 186 residues
- Chains
- 6
- Method
- solid-state nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-endorphin
- UniProt
- P01189
Structure
solid-state nmr · 1 distinct chain · 0% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F | Beta-endorphin | protein | 31 | 0% helix, 35% strand | P01189 |
Interfaces
9 interfaces between chains.
- A–B · 1384 Ų buried · 37 hydrogen bonds · protein-protein
- B–C · 1381 Ų buried · 38 hydrogen bonds · protein-protein
- D–E · 1378 Ų buried · 37 hydrogen bonds · protein-protein
- C–D · 1376 Ų buried · 38 hydrogen bonds · protein-protein
- E–F · 1375 Ų buried · 35 hydrogen bonds · protein-protein
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 P01189
- Elsewhere: RCSB PDB 6TUB · PDBe 6TUB · UniProt P01189
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