Solution conformation of RNA-bound NELF-E RRM. Determined by solution NMR. Released 8 Apr 2008.
Explore 2JX2 in 3D Show helices and sheets RCSB PDB PDBe
2JX2 contains 2 α-helices and 8 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 | 39 | 1 | 1 |
| β-strand | 40-45 | 6 | 2 |
| α-helix | 51-58 | 8 | |
| β-strand | 64-70 | 7 | 2 |
| β-strand | 75-80 | 6 | 2 |
| α-helix | 83-93 | 11 | |
| β-strand | 96-97 | 2 | 3 |
| β-strand | 102-103 | 2 | 3 |
| β-strand | 104-107 | 4 | 2 |
| β-strand | 116 | 1 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Negative elongation factor E | A | protein | 121 | Homo sapiens | P18615 (AlphaFold model) |
>2JX2_1 Negative elongation factor E (chains A) MGSSHHHHHHSSGLVPRGSHMGPFRRSDSFPERRAPRKGNTLYVYGEDMTPTLLRGAFSP FGNIIDLSMDPPRNCAFVTYEKMESADQAVAELNGTQVESVQLKVNIARKQPMLDAATGK S
NELF-E RRM Undergoes Major Structural Changes in Flexible Protein Regions on Target RNA Binding. Rao, J.N., Schweimer, K., Wenzel, S. et al. Biochemistry (2008) 47:3756-3761. DOI 10.1021/bi702429m · PubMed
Other PDB entries of the same protein (UniProt P18615 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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