Research workbench
Cryo-EM structure of murine aa amyloid fibril
Analyse Cryo-EM structure of murine aa amyloid fibril in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6DSO
- Type
- protein
- Length
- 828 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Serum amyloid a-2 protein
- UniProt
- P05367
- Pockets
- 1 · best druggability 0.31
Structure
electron microscopy · 1 distinct chain · 0% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L | Serum amyloid a-2 protein | protein | 69 | 0% helix, 49% strand | P05367 |
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 | 80 | 0.31 | 0.74 | 19 | empty |
Interfaces
29 interfaces between chains.
- G–I · 3042 Ų buried · 84 hydrogen bonds · protein-protein
- H–J · 3038 Ų buried · 84 hydrogen bonds · protein-protein
- A–C · 3034 Ų buried · 84 hydrogen bonds · protein-protein
- C–E · 3032 Ų buried · 86 hydrogen bonds · protein-protein
- D–F · 3031 Ų buried · 86 hydrogen bonds · protein-protein
Compared structures
- 6DSO · Cryo-EM structure of murine AA amyloid fibril · the same entry in another collection · chain L against L, 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 P05367
- Elsewhere: RCSB PDB 6DSO · PDBe 6DSO · UniProt P05367
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