2I32: Anti-Silencing Factor 1 paralog a

Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly. Determined by X-ray diffraction at 2.7 Å resolution. Released 19 Sept 2006.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,910
Mol. weight: 54.11 kDa
Released: 19 Sept 2006

Explore 2I32 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2I32 contains 15 α-helices and 24 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: 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: 7 helices, 9 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	3
β-strand	16-17	2	4
α-helix	21	1
β-strand	22-30	9	3
β-strand	38-45	8	4
α-helix	51-53	3
β-strand	54-62	9	4
β-strand	68-76	9	3
α-helix	77-79	3
α-helix	81-83	3
α-helix	86-89	4
β-strand	91-101	11	4
β-strand	104-117	14	4
α-helix	120-124	5
α-helix	132-134	3
β-strand	135-148	14	4

Chain E: 1 helix, 3 β-strands

Element	Residues	Length	Sheet
β-strand	450-453	4	2
β-strand	459-462	4	2
α-helix	463	1
β-strand	464-465	2	1

Chain F: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	450-453	4	4
β-strand	459-462	4	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Anti-Silencing Factor 1 paralog a	A, B	protein	182	Homo sapiens	Q9Y294 (AlphaFold model)
Histone Regulatory homolog A	E, F	protein	57	Homo sapiens	P54198 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2I32_1 Anti-Silencing Factor 1 paralog a (chains A, B)
MGSSHHHHHHDYDIPTTENLYFQGSMAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLS
EDLEWKIIYVGSAESEEYDQVLDSVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVV
LITCTYRGQEFIRVGYYVNNEYTETELRENPPVKPDFSKLQRNILASNPRVTRFHINWED
NT

Sequence of entity 2 (E, F), FASTA

>2I32_2 Histone Regulatory homolog A (chains E, F)
SENLYFQGSSATSVAGVVNGESLEDIRKNLLKKQVETRTADGRRRITPLCIAQLDTG

Primary citation

Structure of a human ASF1a-HIRA complex and insights into specificity of histone chaperone complex assembly. Tang, Y., Poustovoitov, M.V., Zhao, K. et al. Nat Struct Mol Biol (2006) 13:921-929. DOI 10.1038/nsmb1147 · 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
2IO5 2.7 Å, Crystal structure of the CIA- histone H3-H4 complex

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