2idc Summary

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Structure of the Histone H3-Asf1 Chaperone Interaction

The structure was published by Antczak, A.J., Tsubota, T., Kaufman, P.D., and Berger, J.M., in 2006 in a paper entitled "Structure of the yeast histone H3-ASF1 interaction: implications for chaperone mechanism, species-specific interactions, and epigenetics." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 2006.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of Anti-silencing protein 1 and Histone H3 Chimera. This molecule has the UniProt identifier P32447 (ASF1_YEAST)search. The sample contained 179 residues which is < 90% of the natural sequence. Out of 179 residues 167 were observed and are deposited in the PDB.

The molecule is most likely monomeric.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Anti-silencing protein 1 and Histone H3 Chimera P32447 (2-155) (ASF1_YEAST)search ,
P61830 (119-135) (H3_YEAST)search
Saccharomyces cerevisiae S288csearch ,
Saccharomyces cerevisiae S288csearch
< 90% ,
99%
179 93%


Chain Structural classification (CATH) Sequence family (Pfam)
A (P61830) ASF1-likesearch PF00125: Core histone H2A/H2B/H3/H4search

Chain ID Cellular component (GO) Biological process (GO)
A (P32447P61830) nucleussearch chromatin assembly or disassemblysearch

Chain InterPro annotation
A Histone chaperone, ASF1-likesearch