Research workbench
Cross-alpha amyloid-like structure alphaama
Analyse Cross-alpha amyloid-like structure alphaama in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6O3N
- Type
- protein
- Length
- 384 residues
- Chains
- 16
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cross-alpha amyloid-like structure alphaama
- Pockets
- 1 · best druggability 0.45
Structure
x-ray diffraction · 1 distinct chain · 92% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P | Cross-alpha amyloid-like structure alphaama | protein | 24 | 92% helix, 0% strand | — |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 64 | 0.45 | 0.82 | 17 | empty |
Interfaces
36 interfaces between chains.
- A–B · 561 Ų buried · 0 hydrogen bonds · protein-protein
- C–D · 549 Ų buried · 0 hydrogen bonds · protein-protein
- I–J · 524 Ų buried · 0 hydrogen bonds · protein-protein
- E–F · 521 Ų buried · 0 hydrogen bonds · protein-protein
- K–L · 488 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 6O3N · Cross-alpha Amyloid-like Structure alphaAmA · 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
- Elsewhere: RCSB PDB 6O3N · PDBe 6O3N
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