2IO5: CIA- histone H3-H4 complex

Crystal structure of the CIA- histone H3-H4 complex. Determined by X-ray diffraction at 2.7 Å resolution. Released 27 Feb 2007.

Method: X-ray diffraction
Resolution: 2.7 Å
Organisms: Homo sapiens, Xenopus laevis
Chains: 3
Atoms: 2,474
Mol. weight: 46.38 kDa
Released: 27 Feb 2007

Explore 2IO5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2IO5 contains 14 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: 7 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
β-strand	68-76	9	1
α-helix	77-79	3
α-helix	81-83	3
α-helix	86-89	4
β-strand	91-101	11	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	64-78	15
β-strand	83	1	3
α-helix	86-113	28
β-strand	118-119	2	4
α-helix	121-131	11

Chain C: 4 helices, 3 β-strands

Element	Residues	Length	Sheet
α-helix	31-40	10
β-strand	45-46	2	4
α-helix	50-74	25
β-strand	80	1	3
α-helix	81-82	2
α-helix	83-91	9
β-strand	95-97	3	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
ASF1A protein	A	protein	175	Homo sapiens	Q9Y294 (AlphaFold model)
Histone H3.1	B	protein	135	Xenopus laevis	P84233 (AlphaFold model)
Histone H4	C	protein	102	Xenopus laevis	P62799 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2IO5_1 ASF1A protein (chains A)
GSHMAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVL
DSVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEY
TETELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDNTEKLEDAESSNPNLQS

Sequence of entity 2 (B), FASTA

>2IO5_2 Histone H3.1 (chains B)
ARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTEL
LIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIM
PKDIQLARRIRGERA

Sequence of entity 3 (C), FASTA

>2IO5_3 Histone H4 (chains C)
SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKV
FLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG

Primary citation

Structure and function of the histone chaperone CIA/ASF1 complexed with histones H3 and H4. Natsume, R., Eitoku, M., Akai, Y. et al. Nature (2007) 446:338-341. DOI 10.1038/nature05613 · PubMed

Other PDB entries of the same protein (UniProt Q9Y294 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9SVO 1.6 Å, Crystal structure hASF1A 156-cr5
9TRB 1.65 Å, Crystal structure hASF1A 156-cr13
9SQK 1.7 Å, Crystal structure hASF1A 156-cr17
6ZUF 1.8 Å, Urea-based Foldamer Inhibitor chimera C2 in complex with ASF1 Histone chaperone
6F0H 1.98 Å, Crystal structure ASF1-ip4
9SS3 2.0 Å, Crystal structure hASF1A 156-cr7
6F0F 2.0 Å, Crystal structure ASF1-ip2_s
7LNY 2.1 Å, Apo structure of the Histone chaperone ASF1A residues 1-155
8CJ2 2.13 Å, Urea-based foldamer inhibitor c3u_5 chimera in complex with ASF1 histone chaperone
6F0G 2.3 Å, Crystal structure ASF1-ip3
8CJ1 2.56 Å, Urea-based foldamer inhibitor c3u_3 chimera in complex with ASF1 histone chaperone
2I32 2.7 Å, Structure of a human ASF1a-HIRA complex and insights into specificity of histone…

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