Structure of the Ran-binding domain from human RanBP3 (wild type). Determined by X-ray diffraction at 2.1 Å resolution. Released 16 Feb 2011.
Explore 2Y8F in 3D Show helices and sheets RCSB PDB PDBe
2Y8F contains 5 α-helices and 28 β-strands across 4 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 | 329-344 | 16 | 1 |
| β-strand | 349-364 | 16 | 1 |
| β-strand | 370-379 | 10 | 1 |
| β-strand | 385-390 | 6 | 1 |
| β-strand | 397-401 | 5 | 1 |
| β-strand | 404-410 | 7 | 1 |
| β-strand | 417-423 | 7 | 1 |
| α-helix | 426-444 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 331-344 | 14 | 2 |
| β-strand | 349-362 | 14 | 2 |
| β-strand | 373-379 | 7 | 2 |
| β-strand | 385-390 | 6 | 2 |
| β-strand | 397-401 | 5 | 2 |
| β-strand | 404-410 | 7 | 2 |
| β-strand | 417-423 | 7 | 2 |
| α-helix | 426-449 | 24 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 331-344 | 14 | 3 |
| β-strand | 349-363 | 15 | 3 |
| β-strand | 372-379 | 8 | 3 |
| β-strand | 385-390 | 6 | 3 |
| β-strand | 397-401 | 5 | 3 |
| β-strand | 404-411 | 8 | 3 |
| β-strand | 416-423 | 8 | 3 |
| α-helix | 426-444 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 322-325 | 4 | |
| β-strand | 331-344 | 14 | 4 |
| β-strand | 349-363 | 15 | 4 |
| β-strand | 372-379 | 8 | 4 |
| β-strand | 385-390 | 6 | 4 |
| β-strand | 397-401 | 5 | 4 |
| β-strand | 404-411 | 8 | 4 |
| β-strand | 416-423 | 8 | 4 |
| α-helix | 426-453 | 28 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ran-binding protein 3 | A, B, C, D | protein | 138 | HOMO SAPIENS | Q9H6Z4 (AlphaFold model) |
>2Y8F_1 RAN-BINDING PROTEIN 3 (chains A, B, C, D) GAMKVEVITGEEAESNVLQMQCKLFVFDKTSQSWVERGRGLLRLNDMASTDDGTLQSRLV MRTQGSLRLILNTKLWAQMQIDKASEKSIRITAMDTEDQGVKVFLISASSKDTGQLYAAL HHRILALRSRVEQEQEAK
Insights Into the Function of the Crm1 Cofactor Ranbp3 from the Structure of its Ran-Binding Domain. Langer, K., Dian, C., Rybin, V. et al. PLoS One (2011) 6:17011. DOI 10.1371/JOURNAL.PONE.0017011 · PubMed
Other PDB entries of the same protein (UniProt Q9H6Z4 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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