29UQ: KAT6A surface mutant

KAT6A surface mutant in complex with co-factor acetyl-co-a. Determined by X-ray diffraction at 2.13 Å resolution. Released 9 Sept 2026.

Method: X-ray diffraction
Resolution: 2.13 Å
Organism: Homo sapiens
Chains: 4
Atoms: 9,986
Mol. weight: 133.22 kDa
Ligands: ACO, ZN
Released: 9 Sept 2026

Explore 29UQ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

29UQ contains 48 α-helices and 64 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.

Chains AAA, CCC and DDD: 12 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	511-514	4	1
β-strand	517-520	4	1
α-helix	529-532	4
β-strand	536-539	4	1
β-strand	546-547	2	1
α-helix	550-559	10
β-strand	568-573	6	2
β-strand	576-582	7	2
α-helix	587-598	12
β-strand	613-622	10	2
β-strand	625-635	11	2
β-strand	642-644	3	3
β-strand	647-649	3	2
α-helix	651-653	3
α-helix	658-673	16
β-strand	677	1	4
β-strand	678-679	2	3
α-helix	680	1
α-helix	683-684	2
α-helix	685-705	21
α-helix	713-720	8
β-strand	722	1	4
α-helix	724-733	10
β-strand	737-739	3	5
β-strand	744-746	3	5
α-helix	750-763	14
α-helix	771-773	3
β-strand	774	1	2

Chain BBB: 12 helices, 16 β-strands

Element	Residues	Length	Sheet
β-strand	511-514	4	6
β-strand	517-520	4	6
α-helix	529-532	4
β-strand	536-539	4	6
β-strand	546-547	2	6
α-helix	550-559	10
β-strand	568-573	6	7
β-strand	576-582	7	7
α-helix	587-598	12
β-strand	613-622	10	7
β-strand	625-635	11	7
β-strand	642-644	3	8
β-strand	647-649	3	7
α-helix	651-653	3
α-helix	658-673	16
β-strand	677	1	9
β-strand	678-679	2	8
α-helix	680	1
α-helix	683-684	2
α-helix	685-705	21
α-helix	713-720	8
β-strand	722	1	9
α-helix	724-733	10
β-strand	737-740	4	10
β-strand	743-746	4	10
α-helix	750-763	14
α-helix	771-773	3
β-strand	774	1	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone acetyltransferase KAT6A	AAA, BBB, CCC, DDD	protein	272	Homo sapiens	Q92794 (AlphaFold model)

Sequence of entity 1 (AAA, BBB, CCC, DDD), FASTA

>29UQ_1 Histone acetyltransferase KAT6A (chains AAA, BBB, CCC, DDD)
GSPSVIEFGKYEIHTWYSSPYPQEYSRLPKLYLCEFCLKYMKSRTILQQHMKKCGWFHPP
ANEIYRKNNISVFEVDGNVSTIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTQNDVKGC
HLVGYFSKEKHSQQKYNVSSIMILPQYQRKGYGRFLIDFSYLLSKREGQAGSPEKPLSDL
GRLSYMAYWKSVILECLYHQNDKQISIKKLSKLTGISPQDITSTLHHLRMLDFRSDQFVI
IRREKLIQDHMAKLQLNLRPVDVDPESLRWTP

Ligands and cofactors

ID	Name	Formula	Copies
ACO	Acetyl coenzyme *a	C23 H38 N7 O17 P3 S	4
ZN	Zinc ion	Zn	4

Water and common crystallization additives (PEG, GOL) are not listed.

Primary citation

KAT6A-inhibitor co-crystal structures: tackling a challenging crystallization target via two alternative approaches. Puetter, V., Bouche, L., Nowak-Reppel, K. et al. Acta Crystallogr D Struct Biol (2026) 82:1111-1124. DOI 10.1107/S2059798326008545 · PubMed

Other PDB entries of the same protein (UniProt Q92794 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5B78 1.4 Å, Crystal structure of MOZ double PHD finger mutant-S210D/N235R in complex with histone H3…
3V43 1.47 Å, Crystal structure of MOZ
7Y43 1.5 Å, Crystal structure of the KAT6A WH domain and its bound double stranded DNA
5B77 1.55 Å, Crystal structrue of MOZ double PHD finger in complex with histone H3 propionylation at…
4LK9 1.6 Å, Crystal Structure of MOZ double PHD finger histone H3 tail complex
4LKA 1.61 Å, Crystal Structure of MOZ double PHD finger histone H3K9ac complex
5B76 1.65 Å, Crystal structure of MOZ double PHD finger domain in complex with histone H3…
5B75 1.7 Å, Crystal structure of MOZ double PHD finger in complex with histone H3 butyrylation at K14
9DZN 1.72 Å, KAT6A MYST domain complexed with a H3K14-CoA bisubstrate inhibitor
8H7A 1.92 Å, Crystal structure of the dimer form KAT6A WH domain with its bound double stranded DNA
6LSB 2.0 Å, Crystal Structure of DPF domain of MOZ in complex with H3K14bz peptide
9ARR 2.1 Å, Crystal structure of AF9 YEATS domain in complex with dicrotonylated at K1007 and K1014…

Browse structure collections

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