Research workbench
Arml prion fibril
Analyse Arml prion fibril in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7TD6
- Type
- protein
- Length
- 690 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major prion protein
- UniProt
- P04925
- Pockets
- 7 · best druggability 0.75
Structure
electron microscopy · 1 distinct chain · 0% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1, A, B, C, D | Major prion protein | protein | 138 | 0% helix, 54% strand | P04925 |
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 476 | 0.75 | 0.84 | 63 | empty |
| 2 | 193 | 0.70 | 0.88 | 32 | empty |
| 3 | 131 | 0.65 | 0.88 | 31 | empty |
| 4 | 65 | 0.63 | 0.92 | 31 | empty |
| 5 | 52 | 0.57 | 0.91 | 25 | empty |
Interfaces
7 interfaces between chains.
- A–C · 6249 Ų buried · 182 hydrogen bonds · protein-protein
- 1–A · 6243 Ų buried · 184 hydrogen bonds · protein-protein
- C–D · 6238 Ų buried · 180 hydrogen bonds · protein-protein
- 1–B · 6225 Ų buried · 175 hydrogen bonds · protein-protein
- A–D · 104 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 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 P04925
- Elsewhere: RCSB PDB 7TD6 · PDBe 7TD6 · UniProt P04925
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