Solution structure of RRM domain in A18 hnRNP. Determined by solution NMR. Released 16 Nov 2005.
Explore 1X5S in 3D Show helices and sheets RCSB PDB PDBe
1X5S contains 2 α-helices and 4 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 | 14-18 | 5 | 1 |
| α-helix | 26-36 | 11 | |
| β-strand | 41-44 | 4 | 1 |
| β-strand | 56-60 | 5 | 1 |
| α-helix | 64-74 | 11 | |
| β-strand | 85-90 | 6 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Cold-inducible RNA-binding protein | A | protein | 102 | Homo sapiens | Q14011 (AlphaFold model) |
>1X5S_1 Cold-inducible RNA-binding protein (chains A) GSSGSSGMASDEGKLFVGGLSFDTNEQSLEQVFSKYGQISEVVVVKDRETQRSRGFGFVT FENIDDAKDAMMAMNGKSVDGRQIRVDQAGKSSDNRSGPSSG
Solution structure of RRM domain in A18 hnRNP. Sato, A., Muto, Y., Inoue, M. et al. To be published.
Other PDB entries of the same protein (UniProt Q14011 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1X5S directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.