Research workbench
NMR studies of a pathogenic mutant (D178N) of the human prion protein
Analyse NMR studies of a pathogenic mutant (D178N) of the human prion protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2K1D
- Type
- protein
- Length
- 107 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major prion protein
- UniProt
- P04156
- Pockets
- 1 · best druggability 0.56
Structure
solution nmr · 1 distinct chain · 57% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Major prion protein | protein | 107 | 57% helix, 0% strand | P04156 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 226 | 0.56 | 0.78 | 26 | empty |
Compared structures
- 2K1D · NMR Studies of a Pathogenic Mutant (D178N) of the Human Prion Protein · the same entry in another collection · chain A against A, TM-score 1.00
- P04156 · AlphaFold monomer V2.0 prediction for major prion protein (P04156) · a predicted model of the same protein · chain A against A, TM-score 0.67
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 P04156
- Elsewhere: RCSB PDB 2K1D · PDBe 2K1D · UniProt P04156
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