9ARO: AF9 YEATS domain

Crystal structure of AF9 YEATS domain in complex with acetylated at K1007 MOZ. Determined by X-ray diffraction at 2.3 Å resolution. Released 22 Jan 2025.

Method
X-ray diffraction
Resolution
2.3 Å
Organism
Homo sapiens
Chains
8
Atoms
4,880
Mol. weight
67.66 kDa
Released
22 Jan 2025

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

Secondary structure: helices and β-sheets

9ARO contains 16 α-helices and 36 β-strands across 8 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: 4 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand4-19161
β-strand30-3781
α-helix39-413
α-helix44-463
β-strand48-5472
β-strand63-6642
β-strand71-7771
β-strand81-8992
β-strand97-10482
α-helix112-1132
β-strand114-125121
α-helix129-1379
Chains B and D: 4 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand3-19171
β-strand30-3781
α-helix39-413
α-helix44-463
β-strand48-5473
β-strand63-6643
β-strand71-7771
β-strand81-8993
β-strand97-10483
α-helix112-1132
β-strand114-125121
α-helix129-1379
Chain C: 4 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand3-19174
β-strand30-3784
α-helix44-463
β-strand48-5475
β-strand63-6645
β-strand71-7774
β-strand81-8995
β-strand97-10485
α-helix107-1082
α-helix112-1132
β-strand114-125124
α-helix129-1379
Chains E, F, G and H: 0 helices, 1 β-strand
ElementResiduesLengthSheet
β-strand213

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein AF-9A, B, C, Dprotein138Homo sapiensP42568 (AlphaFold model)
Acetylated Peptide from Histone acetyltransferase KAT6AE, F, G, Hprotein4Homo sapiensQ92794 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>9ARO_1 Protein AF-9 (chains A, B, C, D)
MASSCAVQVKLELGHRAQVRKKPTVEGFTHDWMVFVRGPEHSNIQHFVEKVVFHLHESFP
RPKRVCKDPPYKVEESGYAGFILPIEVYFKNKEEPRKVRFDYDLFLHLEGHPPVNHLRCE
KLTFNNPTEDFRRKLLKA
Sequence of entity 2 (E, F, G, H), FASTA
>9ARO_2 Acetylated Peptide from Histone acetyltransferase KAT6A (chains E, F, G, H)
LTKP

Primary citation

A multivalent engagement of ENL with MOZ. Becht, D.C., Selvam, K., Lachance, C. et al. Nat Struct Mol Biol (2025) 32:709-718. DOI 10.1038/s41594-024-01455-8 · PubMed

Other PDB entries of the same protein (UniProt P42568 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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