2IDC: Histone H3-Asf1 Chaperone Interaction

Structure of the Histone H3-Asf1 Chaperone Interaction. Determined by X-ray diffraction at 2.2 Å resolution. Released 30 Jan 2007.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Saccharomyces cerevisiae
Chains: 1
Atoms: 1,429
Mol. weight: 20.08 kDa
Released: 30 Jan 2007

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

Secondary structure: helices and β-sheets

2IDC contains 7 α-helices and 10 β-strands across 1 chain. 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	4-12	9	1
β-strand	16-17	2	2
α-helix	21	1
β-strand	22-30	9	1
β-strand	38-44	7	2
α-helix	51-53	3
β-strand	55-62	8	2
β-strand	68-76	9	1
α-helix	77-79	3
α-helix	81-83	3
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
α-helix	166-173	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Anti-silencing protein 1 and histone H3 chimera	A	protein	179	Saccharomyces cerevisiae	P32447 (AlphaFold model), P61830 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2IDC_1 ANTI-SILENCING PROTEIN 1 AND HISTONE H3 CHIMERA (chains A)
SNASIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHDQELD
SILVGPVPVGVNKFVFSADPPSAELIPASELVSVTVILLSCSYDGREFVRVGYYVNNEYD
EEELRENPPAKVQVDHIVRNILAEKPRVTRFNIVWDNAAGAATAAKKEIKLARRLRGER

Primary citation

Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics. Antczak, A.J., Tsubota, T., Kaufman, P.D. et al. BMC Struct Biol (2006) 6:26-26. DOI 10.1186/1472-6807-6-26 · 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.
2HUE 1.7 Å, Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4
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
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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