1ATR
THREONINE 204 OF THE CHAPERONE PROTEIN HSC70 INFLUENCES THE STRUCTURE OF THE ACTIVE SITE BUT IS NOT ESSENTIAL FOR ATP HYDROLYSIS
Summary for 1ATR
Entry DOI | 10.2210/pdb1atr/pdb |
Descriptor | HEAT-SHOCK COGNATE 70 KD PROTEIN, MAGNESIUM ION, PHOSPHATE ION, ... (5 entities in total) |
Functional Keywords | chaperone protein |
Biological source | Bos taurus (cattle) |
Total number of polymer chains | 1 |
Total formula weight | 43057.54 |
Authors | O'Brien, M.C.,Mckay, D.B. (deposition date: 1993-08-09, release date: 1993-10-31, Last modification date: 2024-02-07) |
Primary citation | O'Brien, M.C.,McKay, D.B. Threonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis. J.Biol.Chem., 268:24323-24329, 1993 Cited by PubMed: 8226982PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.34 Å) |
Structure validation
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