Solution structure of RRM domain in HNRPC protein. Determined by solution NMR. Released 25 Nov 2004.
Explore 1WF2 in 3D Show helices and sheets RCSB PDB PDBe
1WF2 contains 2 α-helices and 6 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 | 18-23 | 6 | 1 |
| α-helix | 30-35 | 6 | |
| β-strand | 43-49 | 7 | 1 |
| β-strand | 51-57 | 7 | 1 |
| α-helix | 60-68 | 9 | |
| β-strand | 74-75 | 2 | 2 |
| β-strand | 78-79 | 2 | 2 |
| β-strand | 81-84 | 4 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Heterogeneous nuclear ribonucleoproteins C1/C2 | A | protein | 98 | Homo sapiens | P07910 (AlphaFold model) |
>1WF2_1 Heterogeneous nuclear ribonucleoproteins C1/C2 (chains A) GSSGSSGKTDPRSMNSRVFIGNLNTLVVKKSDVEAIFSKYGKIVGCSVHKGFAFVQYVNE RNARAAVAGEDGRMIAGQVLDINLAAEPKVNRSGPSSG
Solution structure of RRM domain in HNRPC protein. He, F., Muto, Y., Inoue, M. et al. To be published.
Other PDB entries of the same protein (UniProt P07910 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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