Crystal structure of human nuclear migration protein NudC. Determined by X-ray diffraction at 1.75 Å resolution. Released 27 Apr 2011.
Explore 3QOR in 3D Show helices and sheets RCSB PDB PDBe
3QOR contains 26 α-helices and 70 β-strands across 5 chains. 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 | 159 | 1 | 1 |
| β-strand | 168 | 1 | 2 |
| β-strand | 173-176 | 4 | 2 |
| β-strand | 180-186 | 7 | 2 |
| α-helix | 195-197 | 3 | |
| β-strand | 198-203 | 6 | 3 |
| β-strand | 206-211 | 6 | 3 |
| β-strand | 218-221 | 4 | 3 |
| β-strand | 222 | 1 | 4 |
| β-strand | 226 | 1 | 5 |
| α-helix | 228-230 | 3 | |
| β-strand | 232-236 | 5 | 2 |
| β-strand | 240-246 | 7 | 2 |
| β-strand | 247 | 1 | 5 |
| β-strand | 258 | 1 | 4 |
| α-helix | 262-263 | 2 | |
| β-strand | 264 | 1 | 1 |
| α-helix | 266-268 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 158 | 1 | |
| β-strand | 159 | 1 | 11 |
| α-helix | 160-161 | 2 | |
| β-strand | 168 | 1 | 12 |
| β-strand | 173-176 | 4 | 12 |
| β-strand | 180-186 | 7 | 12 |
| α-helix | 195-197 | 3 | |
| β-strand | 198-203 | 6 | 13 |
| β-strand | 206-211 | 6 | 13 |
| β-strand | 218-221 | 4 | 13 |
| β-strand | 222 | 1 | 14 |
| β-strand | 226 | 1 | 15 |
| α-helix | 228-230 | 3 | |
| β-strand | 232-236 | 5 | 12 |
| β-strand | 240-246 | 7 | 12 |
| β-strand | 247 | 1 | 15 |
| β-strand | 258 | 1 | 14 |
| α-helix | 262-263 | 2 | |
| β-strand | 264 | 1 | 11 |
| α-helix | 266-268 | 3 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 159 | 1 | 21 |
| α-helix | 160-161 | 2 | |
| β-strand | 167-168 | 2 | 12 |
| β-strand | 173-176 | 4 | 12 |
| β-strand | 180-186 | 7 | 12 |
| α-helix | 195-197 | 3 | |
| β-strand | 198-203 | 6 | 22 |
| β-strand | 206-211 | 6 | 22 |
| β-strand | 218-221 | 4 | 22 |
| β-strand | 222 | 1 | 23 |
| β-strand | 226 | 1 | 24 |
| α-helix | 228-230 | 3 | |
| β-strand | 232-236 | 5 | 12 |
| β-strand | 240-246 | 7 | 12 |
| β-strand | 247 | 1 | 24 |
| β-strand | 258 | 1 | 23 |
| α-helix | 262-263 | 2 | |
| β-strand | 264 | 1 | 21 |
| α-helix | 266-268 | 3 | |
| α-helix | 271-273 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Nuclear migration protein nudC | A | protein | 121 | Homo sapiens | Q9Y266 (AlphaFold model) |
| Nuclear migration protein nudC | B | protein | 121 | Homo sapiens | Q9Y266 (AlphaFold model) |
| Nuclear migration protein nudC | C | protein | 121 | Homo sapiens | Q9Y266 (AlphaFold model) |
| Nuclear migration protein nudC | D, E | protein | 121 | Homo sapiens | Q9Y266 (AlphaFold model) |
>3QOR_1 Nuclear migration protein nudC (chains A) GSSSKLKPNLGNGADLPNYRWTQTLSELDLAVPFCVNFRLKGKDMVVDIQRRHLRVGLKG QPAIIDGELYNEVKVEESSWLIADGAVVTVHLEKINKMEWWSRLVSSDPEINTKKINPEN S
>3QOR_2 Nuclear migration protein nudC (chains B) GSSSKLKPNLGNGADLPNYRWTQTLSELDLAVPFCVNFRLKGKDMVVDIQRRHLRVGLKG QPAIIDGELYNEVKVEESSWLIADGAVVTVHLEKINKMEWWSRLVSSDPEINTKKINPEN S
>3QOR_3 Nuclear migration protein nudC (chains C) GSSSKLKPNLGNGADLPNYRWTQTLSELDLAVPFCVNFRLKGKDMVVDIQRRHLRVGLKG QPAIIDGELYNEVKVEESSWLIADGAVVTVHLEKINKMEWWSRLVSSDPEINTKKINPEN S
>3QOR_4 Nuclear migration protein nudC (chains D, E) GSSSKLKPNLGNGADLPNYRWTQTLSELDLAVPFCVNFRLKGKDMVVDIQRRHLRVGLKG QPAIIDGELYNEVKVEESSWLIADGAVVTVHLEKINKMEWWSRLVSSDPEINTKKINPEN S
Structural Features and Chaperone Activity of the NudC Protein Family. Zheng, M., Cierpicki, T., Burdette, A.J. et al. J Mol Biol (2011) 409:722-741. DOI 10.1016/j.jmb.2011.04.018 · PubMed
Other PDB entries of the same protein (UniProt Q9Y266 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 3QOR 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.