Human prion protein. Determined by solution NMR. Released 16 Dec 1999.
Explore 1QLX in 3D Show helices and sheets RCSB PDB PDBe
1QLX contains 5 α-helices and 2 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 129-130 | 2 | 1 |
| α-helix | 144-153 | 10 | |
| β-strand | 162-163 | 2 | 1 |
| α-helix | 173-186 | 14 | |
| α-helix | 187-191 | 5 | |
| α-helix | 192-194 | 3 | |
| α-helix | 200-227 | 28 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Prion protein | A | protein | 210 | HOMO SAPIENS | P04156 (AlphaFold model) |
>1QLX_1 PRION PROTEIN (chains A) GSKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGG WGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIH FGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTE TDVKMMERVVEQMCITQYERESQAYYQRGS
NMR Solution Structure of the Human Prion Protein. Zahn, R., Liu, A., Luhrs, T. et al. Proc Natl Acad Sci U S A (2000) 97:145. DOI 10.1073/PNAS.97.1.145 · PubMed
Other PDB entries of the same protein (UniProt P04156 (AlphaFold model), which also has an AlphaFold model), best resolution first:
1QLX is part of these collections:
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