6VO5: Human histone acetytransferas 1

Crystal structure of Human histone acetytransferas 1 (HAT1) in complex with isobutryl-COA and K12A mutant variant of histone H4. Determined by X-ray diffraction at 1.6 Å resolution. Released 11 Mar 2020.

Method: X-ray diffraction
Resolution: 1.6 Å
Organism: Homo sapiens
Chains: 4
Atoms: 6,547
Mol. weight: 82.37 kDa
Ligands: CO6
Released: 11 Mar 2020

Explore 6VO5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6VO5 contains 37 α-helices and 36 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: 18 helices, 18 β-strands

Element	Residues	Length	Sheet
α-helix	22-25	4
β-strand	26-28	3	1
α-helix	29-32	4
β-strand	33-38	6	2
α-helix	41-44	4
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	97-100	4
α-helix	103-105	3
α-helix	107-112	6
β-strand	120	1	2
α-helix	123-130	8
α-helix	133-135	3
β-strand	141-148	8	4
β-strand	157-164	8	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	252-265	14
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	302-306	5
α-helix	311-321	11
β-strand	323	1	5
α-helix	325-338	14

Chain B: 17 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	51	1	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	97-100	4
α-helix	107-112	6
β-strand	120	1	7
α-helix	123-131	9
α-helix	132-135	4
β-strand	141-148	8	9
β-strand	157-164	8	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	252-265	14
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	325-338	14

Chains C and D: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	15-17	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone acetyltransferase type B catalytic subunit	A, B	protein	324	Homo sapiens	O14929 (AlphaFold model)
Histone H4	C, D	protein	20	Homo sapiens	P62805 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6VO5_1 Histone acetyltransferase type B catalytic subunit (chains A, B)
GSKKLAEYKCNTNTAIELKLVRFPEDLENDIRTFFPEYTHQLFGDDETAFGYKGLKILLY
YIAGSLSTMFRVEYASKVDENFDCVEADDVEGKIRQIIPPGFCTNTNDFLSLLEKEVDFK
PFGTLLHTYSVLSPTGGENFTFQIYKADMTCRGFREYHERLQTFLMWFIETASFIDVDDE
RWHYFLVFEKYNKDGATLFATVGYMTVYNYYVYPDKTRPRVSQMLILTPFQGQGHGAQLL
ETVHRYYTEFPTVLDITAEDPSKSYVKLRDFVLVKLCQDLPCFSREKLMQGFNEDMAIEA
QQKFKINKQHARRVYEILRLLVTD

Sequence of entity 2 (C, D), FASTA

>6VO5_2 Histone H4 (chains C, D)
SGRGKGGKGLGAGGAKRHRK

Ligands and cofactors

ID	Name	Formula	Copies
CO6	Isobutyryl-coenzyme a	C25 H42 N7 O17 P3 S	2

Water and common crystallization additives (UNX, SO4, GOL, ACT) are not listed.

Primary citation

Crystal structure of Human histone acetytransferas 1 (HAT1) in complex with isobutryl-COA and K12A mutant variant of histone H4. Halabelian, L., Zeng, H., Dong, A. et al. To be published.

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

2P0W 1.9 Å, Human histone acetyltransferase 1 (HAT1)
9MJG 2.58 Å, Crystal structure of HAT1 in complex with XS380871

Browse structure collections

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