2HUE: H3-H4 chaperone Asf1

Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4. Determined by X-ray diffraction at 1.7 Å resolution. Released 21 Nov 2006.

Method: X-ray diffraction
Resolution: 1.7 Å
Organisms: Saccharomyces cerevisiae, Xenopus laevis
Chains: 3
Atoms: 3,080
Mol. weight: 38.53 kDa
Ligands: ZN
Released: 21 Nov 2006

Explore 2HUE in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2HUE contains 15 α-helices and 15 β-strands across 3 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: 8 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	1
β-strand	16-17	2	2
α-helix	21	1
β-strand	22-30	9	1
β-strand	38-45	8	2
α-helix	51-53	3
β-strand	54-62	9	2
α-helix	65-66	2
β-strand	68-76	9	1
α-helix	77-80	4
α-helix	81-83	3
α-helix	86-89	4
β-strand	93-101	9	2
β-strand	104-117	14	2
α-helix	120-124	5
α-helix	132-134	3
β-strand	135-139	5	2
β-strand	145-148	4	2

Chain B: 3 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	64-76	13
β-strand	83-84	2	3
α-helix	86-113	28
β-strand	118-119	2	4
α-helix	121-130	10

Chain C: 4 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	22-25	4
α-helix	31-40	10
β-strand	45-46	2	4
α-helix	50-75	26
β-strand	80-81	2	3
α-helix	83-89	7
β-strand	95-98	4	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Anti-silencing protein 1	A	protein	175	Saccharomyces cerevisiae	P32447 (AlphaFold model)
Histone H3	B	protein	77	Xenopus laevis	P84233 (AlphaFold model)
Histone H4	C	protein	84	Xenopus laevis	P62799 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2HUE_1 Anti-silencing protein 1 (chains A)
PLGSPNSSIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHD
QELDSILVGPVPVGVNKFVFSADPPSAELIPASELVSVTVILLSCSYDGREFVRVGYYVN
NEYDEEELRENPPAKVQVDHIVRNILAEKPRVTRFNIVWDNENEGDLYPPEQPGV

Sequence of entity 2 (B), FASTA

>2HUE_2 Histone H3 (chains B)
MALIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVALFEDTNLCAIHAKRVT
IMPKDIQLARRIRGERA

Sequence of entity 3 (C), FASTA

>2HUE_3 Histone H4 (chains C)
MKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKR
KTVTAMDVVYALKRQGRTLYGFGG

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1

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

Primary citation

Structural basis for the histone chaperone activity of asf1. English, C.M., Adkins, M.W., Carson, J.J. et al. Cell (2006) 127:495-508. DOI 10.1016/j.cell.2006.08.047 · PubMed

Other PDB entries of the same protein (UniProt P32447 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1ROC 1.5 Å, Crystal structure of the histone deposition protein Asf1
5UCB 1.52 Å, Structure of antigen-Fab complex with engineered switch residue region.
5UEK 1.7 Å, Structure of antigen-Fab 12E complex with Histone chaperone ASF1
5UEA 1.7 Å, Structure of antigen-Fab complex with Histone chaperone ASF1
6AYZ 2.1 Å, Crystal structure of Asf1-Fab 12E complex
2IDC 2.2 Å, Structure of the Histone H3-Asf1 Chaperone Interaction
4ZBJ 2.25 Å, UBN1 peptide bound to H3.3/H4/Asf1
4EO5 2.35 Å, Yeast Asf1 bound to H3/H4G94P mutant
5EII 2.44 Å, Structural determination of an protein complex of a Fab with increased solubility
6AZ2 2.48 Å, Crystal structure of Asf1-Fab 12E complex
4RRP 2.79 Å, Crystal Structure of the Fab complexed with antigen Asf1p, Northeast Structural Genomics…
9AWE 2.8 Å, The crystal structure of an engineered Protein GF with Human Kappa Fab

Browse structure collections

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