1C3G
S. CEREVISIAE HEAT SHOCK PROTEIN 40 SIS1
Summary for 1C3G
| Entry DOI | 10.2210/pdb1c3g/pdb |
| Descriptor | HEAT SHOCK PROTEIN 40 (2 entities in total) |
| Functional Keywords | beta sheets, short helices, chaperone |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Cellular location | Cytoplasm : P25294 |
| Total number of polymer chains | 1 |
| Total formula weight | 19097.80 |
| Authors | |
| Primary citation | Sha, B.,Lee, S.,Cyr, D.M. The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1. Structure, 8:799-807, 2000 Cited by PubMed Abstract: Molecular chaperone Hsp40 can bind non-native polypeptide and facilitate Hsp70 in protein refolding. How Hsp40 and other chaperones distinguish between the folded and unfolded states of proteins to bind nonnative polypeptides is a fundamental issue. PubMed: 10997899DOI: 10.1107/S090744499900476X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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