Crystal structure of human CAPERalpha UHM bound to SF3b155 ULM5. Determined by X-ray diffraction at 1.74 Å resolution. Released 14 May 2014.
Explore 4OZ1 in 3D Show helices and sheets RCSB PDB PDBe
4OZ1 contains 11 α-helices and 13 β-strands across 3 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 |
|---|---|---|---|
| α-helix | 413-416 | 4 | |
| β-strand | 419-423 | 5 | 1 |
| α-helix | 436-448 | 13 | |
| β-strand | 456-459 | 4 | 1 |
| β-strand | 468-471 | 4 | 1 |
| α-helix | 475-485 | 11 | |
| β-strand | 489-490 | 2 | 2 |
| β-strand | 493-494 | 2 | 2 |
| β-strand | 496-500 | 5 | 1 |
| α-helix | 502-508 | 7 | |
| α-helix | 510-513 | 4 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 419-423 | 5 | 3 |
| α-helix | 428-432 | 5 | |
| α-helix | 436-448 | 13 | |
| β-strand | 456-459 | 4 | 3 |
| β-strand | 468-471 | 4 | 3 |
| α-helix | 475-485 | 11 | |
| β-strand | 489-490 | 2 | 4 |
| β-strand | 493-494 | 2 | 4 |
| β-strand | 496-500 | 5 | 3 |
| α-helix | 502-508 | 7 | |
| α-helix | 510-513 | 4 | |
| α-helix | 518-519 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 338 | 1 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| RNA-binding protein 39 | A, B | protein | 115 | Homo sapiens | Q14498 (AlphaFold model) |
| Splicing factor 3B subunit 1 | C | protein | 10 | Homo sapiens | O75533 (AlphaFold model) |
>4OZ1_1 RNA-binding protein 39 (chains A, B) GSVQPLATQCFQLSNMFNPQTEEEVGWDTEIKDDVIEECNKHGGVIHIYVDKNSAQGNVY VKCPSIAAAIAAVNALHGRWFAGKMITAAYVPLPTYHNLFPDSMTATQLLVPSRR
>4OZ1_2 Splicing factor 3B subunit 1 (chains C) KRKSRWDETP
| ID | Name | Formula | Copies |
|---|---|---|---|
| LYS | Lysine | C6 H15 N2 O2 | 1 |
Water and common crystallization additives (K, CL) are not listed.
Cancer-relevant splicing factor CAPER alpha engages the essential splicing factor SF3b155 in a specific ternary complex. Loerch, S., Maucuer, A., Manceau, V. et al. J Biol Chem (2014) 289:17325-17337. DOI 10.1074/jbc.M114.558825 · PubMed
Other PDB entries of the same protein (UniProt Q14498 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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