Research workbench
Probing the N-terminal beta-sheet conversion in the crystal structure of the full-length human prion protein bound to a Nanobody
Analyse Probing the N-terminal beta-sheet conversion in the crystal structure of the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4KML
- Type
- protein
- Length
- 232 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.5
- Source
- Homo sapiens; Lama glama
- Molecule
- Major prion protein; Nanobody
- UniProt
- P04156
Structure
x-ray diffraction · resolution 1.5 · 2 distinct chains · 32% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Major prion protein | protein | 109 | 58% helix, 12% strand | P04156 |
| B | Nanobody | protein | 123 | 10% helix, 46% strand | — |
Interfaces
1 interface between chains.
- A–B · 662 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 4KML · Probing the N-terminal beta-sheet conversion in the crystal structure of the full-length… · 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 0.94
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 4KML · PDBe 4KML · UniProt P04156
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