Research workbench
Human prion protein variant F198S with M129
Analyse Human prion protein variant F198S with M129 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HES
- Type
- protein
- Length
- 192 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major prion protein
- UniProt
- P04156
- Ligands
- CD
- Pockets
- 1 · best druggability 0.30
Structure
x-ray diffraction · 2 distinct chains · 59% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Major prion protein | protein | 98 | 59% helix, 4% strand | P04156 |
| B | Major prion protein | protein | 94 | 60% helix, 4% strand | P04156 |
Ligands and binding sites
- CD · Cadmium ion · metal · 2 copies · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 59 | 0.30 | 0.75 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 492 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 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 P04156
- Elsewhere: RCSB PDB 3HES · PDBe 3HES · UniProt P04156
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