3TO1
Two surfaces on Rtt106 mediate histone binding and chaperone activity
Summary for 3TO1
| Entry DOI | 10.2210/pdb3to1/pdb |
| Descriptor | Histone chaperone RTT106 (2 entities in total) |
| Functional Keywords | histone chaperone, chaperone |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) |
| Cellular location | Nucleus: P40161 |
| Total number of polymer chains | 2 |
| Total formula weight | 53777.54 |
| Authors | Zunder, R.M.,Antczak, A.J.,Berger, J.M.,Rine, J. (deposition date: 2011-09-02, release date: 2011-12-21, Last modification date: 2024-04-03) |
| Primary citation | Zunder, R.M.,Antczak, A.J.,Berger, J.M.,Rine, J. Two surfaces on the histone chaperone Rtt106 mediate histone binding, replication, and silencing. Proc.Natl.Acad.Sci.USA, 109:E144-E153, 2012 Cited by PubMed: 22198837DOI: 10.1073/pnas.1119095109 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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