Research workbench
Mouse prion protein (121-231) containing the substitutions Y169A, Y225A, and Y226A
Analyse Mouse prion protein (121-231) containing the substitutions Y169A, Y225A, and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2L1K
- Type
- protein
- Length
- 114 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major prion protein
- UniProt
- Q4FJQ7
- Pockets
- 1 · best druggability 0.32
Structure
solution nmr · 1 distinct chain · 47% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Major prion protein | protein | 114 | 47% helix, 4% strand | Q4FJQ7 |
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 | 53 | 0.32 | 0.77 | 12 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 2L1K · Mouse prion protein (121-231) containing the substitutions Y169A, Y225A, and Y226A · 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
- Every structure of UniProt Q4FJQ7
- Elsewhere: RCSB PDB 2L1K · PDBe 2L1K · UniProt Q4FJQ7
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