9MJG: HAT1

Crystal structure of HAT1 in complex with XS380871. Determined by X-ray diffraction at 2.58 Å resolution. Released 5 Feb 2025.

Method: X-ray diffraction
Resolution: 2.58 Å
Organism: Homo sapiens
Chains: 8
Atoms: 20,479
Mol. weight: 306.12 kDa
Ligands: A1BLX
Released: 5 Feb 2025

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

Secondary structure: helices and β-sheets

9MJG contains 125 α-helices and 144 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: 16 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	23-25	3
β-strand	26-28	3	1
α-helix	29-32	4
β-strand	33-38	6	2
α-helix	41-45	5
α-helix	47-49	3
β-strand	50-51	2	2
α-helix	57-60	4
β-strand	65-67	3	1
β-strand	69-70	2	3
β-strand	73-79	7	2
β-strand	85-90	6	2
β-strand	93-94	2	3
α-helix	107-112	6
β-strand	120	1	2
α-helix	123-132	10
α-helix	133-135	3
β-strand	141-149	9	4
β-strand	156-164	9	4
α-helix	171-185	15
β-strand	199-210	12	4
β-strand	213-229	17	4
β-strand	233-243	11	4
α-helix	245-247	3
α-helix	252-264	13
β-strand	270	1	4
β-strand	273	1	5
β-strand	274-275	2	4
α-helix	280-294	15
α-helix	298-300	3
α-helix	302-305	4
α-helix	311-321	11
β-strand	323	1	5
α-helix	325-338	14

Chain B: 16 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	22-25	4
β-strand	26-28	3	6
α-helix	29-32	4
β-strand	33-38	6	7
α-helix	41-45	5
α-helix	47-49	3
β-strand	50-51	2	7
α-helix	57-60	4
β-strand	65-67	3	6
β-strand	69-70	2	8
β-strand	73-79	7	7
β-strand	85-90	6	7
β-strand	93-94	2	8
α-helix	107-112	6
β-strand	120	1	7
α-helix	123-132	10
α-helix	133-135	3
β-strand	141-149	9	9
β-strand	156-164	9	9
α-helix	171-185	15
β-strand	199-210	12	9
β-strand	213-229	17	9
β-strand	233-243	11	9
α-helix	245-247	3
α-helix	252-264	13
β-strand	270	1	9
β-strand	273	1	10
β-strand	274-275	2	9
α-helix	280-294	15
α-helix	298-300	3
α-helix	302-306	5
α-helix	311-321	11
β-strand	323	1	10
α-helix	325-339	15

Chains C and H: 15 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	26-28	3	11
α-helix	29-32	4
β-strand	33-38	6	12
α-helix	41-45	5
α-helix	47-49	3
β-strand	50-51	2	12
α-helix	57-60	4
β-strand	65-67	3	11
β-strand	69-70	2	13
β-strand	73-79	7	12
β-strand	85-90	6	12
β-strand	93-94	2	13
α-helix	107-112	6
β-strand	120	1	12
α-helix	123-132	10
α-helix	133-135	3
β-strand	141-149	9	14
β-strand	156-164	9	14
α-helix	171-185	15
β-strand	199-210	12	14
β-strand	213-229	17	14
β-strand	233-243	11	14
α-helix	245-247	3
α-helix	252-264	13
β-strand	270	1	14
β-strand	273	1	15
β-strand	274-275	2	14
α-helix	280-294	15
α-helix	298-300	3
α-helix	302-306	5
α-helix	311-321	11
β-strand	323	1	15
α-helix	325-339	15

Chains D, F and G: 16 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	23-25	3
β-strand	26-28	3	16
α-helix	29-32	4
β-strand	33-38	6	17
α-helix	41-45	5
α-helix	47-49	3
β-strand	50-51	2	17
α-helix	57-60	4
β-strand	65-67	3	16
β-strand	69-70	2	18
β-strand	73-79	7	17
β-strand	85-90	6	17
β-strand	93-94	2	18
α-helix	107-112	6
β-strand	120	1	17
α-helix	123-132	10
α-helix	133-135	3
β-strand	141-149	9	19
β-strand	156-164	9	19
α-helix	171-185	15
β-strand	199-210	12	19
β-strand	213-229	17	19
β-strand	233-243	11	19
α-helix	245-247	3
α-helix	252-264	13
β-strand	270	1	19
β-strand	273	1	20
β-strand	274-275	2	19
α-helix	280-294	15
α-helix	298-300	3
α-helix	302-306	5
α-helix	311-321	11
β-strand	323	1	20
α-helix	325-338	14

Chain E: 15 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	26-28	3	21
α-helix	29-32	4
β-strand	33-38	6	22
α-helix	41-45	5
α-helix	47-49	3
β-strand	50-51	2	22
α-helix	57-60	4
β-strand	65-67	3	21
β-strand	69-70	2	23
β-strand	73-79	7	22
β-strand	85-90	6	22
β-strand	93-94	2	23
α-helix	107-112	6
β-strand	120	1	22
α-helix	123-132	10
α-helix	133-135	3
β-strand	141-149	9	24
β-strand	156-164	9	24
α-helix	171-185	15
β-strand	199-210	12	24
β-strand	213-229	17	24
β-strand	233-243	11	24
α-helix	245-247	3
α-helix	252-264	13
β-strand	270	1	24
β-strand	273	1	25
β-strand	274-275	2	24
α-helix	280-294	15
α-helix	298-300	3
α-helix	302-306	5
α-helix	311-321	11
β-strand	323	1	25
α-helix	325-338	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone acetyltransferase type B catalytic subunit	A, B, C, D, E, F, G, H	protein	322	Homo sapiens	O14929 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F, G, H), FASTA

>9MJG_1 Histone acetyltransferase type B catalytic subunit (chains A, B, C, D, E, F, G, H)
KKLAEYKCNTNTAIELKLVRFPEDLENDIRTFFPEYTHQLFGDDETAFGYKGLKILLYYI
AGSLSTMFRVEYASKVDENFDCVEADDVEGKIRQIIPPGFCTNTNDFLSLLEKEVDFKPF
GTLLHTYSVLSPTGGENFTFQIYKADMTCRGFREYHERLQTFLMWFIETASFIDVDDERW
HYFLVFEKYNKDGATLFATVGYMTVYNYYVYPDKTRPRVSQMLILTPFQGQGHGAQLLET
VHRYYTEFPTVLDITAEDPSKSYVKLRDFVLVKLCQDLPCFSREKLMQGFNEDMAIEAQQ
KFKINKQHARRVYEILRLLVTD

Ligands and cofactors

ID	Name	Formula	Copies
A1BLX	(4S,7R)-4-(3-ethoxy-4-hydroxy-5-nitrophenyl)-7-(4-fluorophenyl)-4,6,7,8-tetrahy…	C23 H21 F N2 O6	8

Primary citation

Enantioselective protein affinity selection mass spectrometry (E-ASMS). Wang, X., Sun, J., Ahmad, S. et al. Nat Commun (2025) 17:651-651. DOI 10.1038/s41467-025-67403-2 · PubMed

Other PDB entries of the same protein (UniProt O14929 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6VO5 1.6 Å, Crystal structure of Human histone acetytransferas 1 (HAT1) in complex with…
2P0W 1.9 Å, Human histone acetyltransferase 1 (HAT1)

Browse structure collections

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