9VEA: The MIDN Catch-IRF4 (A8I) fusion protein

The MIDN Catch-IRF4 (A8I) fusion protein. Determined by X-ray diffraction at 3.6 Å resolution. Released 4 Feb 2026.

Method
X-ray diffraction
Resolution
3.6 Å
Organism
Homo sapiens
Chains
2
Atoms
892
Mol. weight
15.06 kDa
Released
4 Feb 2026

Explore 9VEA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9VEA contains 5 α-helices and 8 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.

Chain A: 2 helices, 5 β-strands

ElementResiduesLengthSheet
α-helix114-1218
α-helix126-1349
β-strand139-14131
β-strand14412
β-strand14912
β-strand151-15661
β-strand167-17481
Chain B: 3 helices, 3 β-strands
ElementResiduesLengthSheet
β-strand268-26921
β-strand273-27641
β-strand279-28681
α-helix303-31614
α-helix317-3193
α-helix325-3295

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Midnolin,Interferon regulatory factor 4Aprotein66Homo sapiensQ15306 (AlphaFold model), Q504T8 (AlphaFold model)
MidnolinBprotein74Homo sapiensQ504T8 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9VEA_1 Midnolin,Interferon regulatory factor 4 (chains A)
PEQSVMQALESLTETQVSDFLSGRSPLTLALRVGDHMMFVQLQLAWPACENGCQVTGTFY
ICAPPE
Sequence of entity 2 (B), FASTA
>9VEA_2 Midnolin (chains B)
PGAVIESFVNHAPGVFSGTFSGTLHPNCQDSSGRPRRDIGTILQILNDLLSATRHYQGMP
PSLAQLRCHAGSGS

Primary citation

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:

Browse structure collections

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