MolNFT v1 · #151141 · protein
Mouse prion protein in complex with nanobody 484
6HER · Major prion protein: “Mouse prion protein in complex with nanobody 484”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.31). MolNFT v1 #151141 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6HER
- Type
- protein
- Length
- 227 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major prion protein; Nanobody 484
- UniProt
- P04925
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.31
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Major prion protein | protein | 103 | 59% helix, 7% strand | P04925 |
| B | Nanobody 484 | protein | 124 | 12% helix, 45% strand | — |
Ligands and binding sites
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 | 67 | 0.31 | 0.75 | 17 | SO4 |
Interfaces
1 interface between chains.
- A–B · 695 Ų buried · 18 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 P04925
- Elsewhere: RCSB PDB 6HER · PDBe 6HER · UniProt P04925
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