The MIDN Catch-IRF4 (V2Y) fusion protein. Determined by X-ray diffraction at 3.2 Å resolution. Released 4 Feb 2026.
Explore 9VE5 in 3D Show helices and sheets RCSB PDB PDBe
9VE5 contains 6 α-helices and 5 β-strands across 2 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 | 112-123 | 12 | |
| α-helix | 126-133 | 8 | |
| β-strand | 139-143 | 5 | 1 |
| β-strand | 150-156 | 7 | 1 |
| α-helix | 157 | 1 | |
| β-strand | 166-174 | 9 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 266-276 | 11 | 1 |
| β-strand | 279-287 | 9 | 1 |
| α-helix | 290-292 | 3 | |
| α-helix | 303-317 | 15 | |
| α-helix | 325-328 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Midnolin,Interferon regulatory factor 4 | A | protein | 68 | Homo sapiens | Q15306 (AlphaFold model), Q504T8 (AlphaFold model) |
| Midnolin | B | protein | 73 | Homo sapiens | Q504T8 (AlphaFold model) |
>9VE5_1 Midnolin,Interferon regulatory factor 4 (chains A) SRPEQSVMQALESLTETQVSDFLSGRSPLTLALRVGDHMMFVQLQLAWPACENGCQYTGT FYACAPPE
>9VE5_2 Midnolin (chains B) PGAVIESFVNHAPGVFSGTFSGTLHPNCQDSSGRPRRDIGTILQILNDLLSATRHYQGMP PSLAQLRCHAGSG
Biochemical and structural studies of the midnolin Catch domain bound with both wild-type and mutant IRF4 peptides reveal the molecular basis for its broad substrate specificity. Zhong, Y., Chen, Z., Wang, G. et al. Acta Biochim Biophys Sin (Shanghai) (2026) 58:1235-1249. DOI 10.3724/abbs.2026002 · PubMed
Other PDB entries of the same protein (UniProt Q15306 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 9VE5 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.