Solution structure of RRM domain in Parp14. Determined by solution NMR. Released 16 Nov 2005.
Explore 1X5P in 3D Show helices and sheets RCSB PDB PDBe
1X5P 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 | 17-21 | 5 | 1 |
| α-helix | 27-34 | 8 | |
| β-strand | 40-46 | 7 | 1 |
| β-strand | 51-56 | 6 | 1 |
| α-helix | 59-68 | 10 | |
| β-strand | 72-74 | 3 | 2 |
| β-strand | 77-79 | 3 | 2 |
| β-strand | 80-82 | 3 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Negative elongation factor E | A | protein | 97 | Homo sapiens | P18615 (AlphaFold model) |
>1X5P_1 Negative elongation factor E (chains A) GSSGSSGERRAPRKGNTLYVYGEDMTPTLLRGAFSPFGNIIDLSMDPPRNCAFVTYEKME SADQAVAELNGTQVESVQLKVNIARKQPMLDSGPSSG
Solution structure of RRM domain in Parp14. Dang, W., Muto, Y., Inoue, M. et al. To be published.
Other PDB entries of the same protein (UniProt P18615 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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