MolNFT v1 · #89851 · protein
Fragment of human prion protein
4E1H · Major prion protein: “Fragment of human prion protein”. X-ray diffraction, 1 ligand (FE). MolNFT v1 #89851 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4E1H
- Type
- protein
- Length
- 72 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major prion protein
- UniProt
- P04156
- Ligands
- FE
Structure
x-ray diffraction · 2 distinct chains · 0% helix, 67% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E, G, I, K | Major prion protein | protein | 6 | 0% helix, 67% strand | P04156 |
| B, D, F, H, J, L | Major prion protein | protein | 6 | 0% helix, 67% strand | P04156 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
47 interfaces between chains.
- B–D · 323 Ų buried · 4 hydrogen bonds · protein-protein
- F–H · 314 Ų buried · 7 hydrogen bonds · protein-protein
- I–J · 312 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 310 Ų buried · 8 hydrogen bonds · protein-protein
- K–L · 304 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 4E1H · Fragment of human prion protein · 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 P04156
- Elsewhere: RCSB PDB 4E1H · PDBe 4E1H · UniProt P04156
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