9VC7: Zinc finger MYND domain-containing protein 11

Structural insights into the tumor suppressor ZMYND11 reveal diverse recognition mechanisms. Determined by X-ray diffraction at 3.35 Å resolution. Released 14 Jan 2026.

Method: X-ray diffraction
Resolution: 3.35 Å
Organism: Homo sapiens
Chains: 4
Atoms: 3,769
Mol. weight: 60.46 kDa
Ligands: ZN
Released: 14 Jan 2026

Explore 9VC7 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9VC7 contains 13 α-helices and 18 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.

Chain A: 3 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	490-557	68
β-strand	562	1	1
β-strand	569	1	1
β-strand	572-575	4	2
β-strand	578-580	3	2
α-helix	583-592	10
α-helix	594-596	3

Chain B: 3 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	492-558	67
β-strand	562	1	3
β-strand	563	1	4
β-strand	569	1	3
β-strand	572-575	4	4
β-strand	578-580	3	4
α-helix	583-592	10
α-helix	594-596	3

Chain C: 3 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	488-558	71
β-strand	562	1	5
β-strand	569	1	5
β-strand	572-575	4	6
β-strand	578-580	3	6
α-helix	583-589	7
α-helix	590-594	5

Chain D: 4 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	488-558	71
β-strand	562	1	7
β-strand	563	1	8
β-strand	569	1	7
α-helix	570	1
β-strand	572-575	4	8
β-strand	578-580	3	8
α-helix	583-589	7
α-helix	590-594	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Zinc finger MYND domain-containing protein 11	A, B, C, D	protein	122	Homo sapiens	Q15326 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>9VC7_1 Zinc finger MYND domain-containing protein 11 (chains A, B, C, D)
RMKSDHKRETERVVREALEKLRSEMEEEKRQAVNKAVANMQGEMDRKCKQVKEKCKEEFV
EEIKKLATQHKQLISQTKKKQWCYNCEEEAMYHCCWNTSYCSIKCQQEHWHAEHKRTCRR
KR

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	8

Primary citation

Novel intermolecular zinc fingers and redox-driven conformational changes dictate tumor suppressor ZMYND11's role in cooperative recognition of diverse targets. Bai, X., Zhang, J., Wang, S. et al. Nucleic Acids Res (2026) 54. DOI 10.1093/nar/gkag048 · PubMed

Other PDB entries of the same protein (UniProt Q15326 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8XU6 1.63 Å, Structural Insights into the Tumor Suppressor ZMYND11 Reveal Diverse Recognition…
9LOM 1.63 Å, Study on the structure and function of tumor suppressor ZMYND11
9LOA 1.8 Å, Structural insights into the tumor suppressor ZMYND11 reveal diverse recognition…
9M0U 1.89 Å, Structural insights into the tumor suppressor ZMYND11 reveal diverse recognition…
4NS5 1.9 Å, Crystal structure of human BS69 Bromo-Zinc finger-PWWP
5HDA 2.39 Å, Crystal Structure of the BS69 coiled coil-MYND domains bound to an EBNA2 PXLXP motif
9LP4 2.96 Å, Structural insights into the Tumor suppressor ZMYND11 reveal diverse recognition…

Browse structure collections

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