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Structure paper

TitleThreonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis.
Journal, issue, pagesJ. Biol. Chem., Vol. 268, Page 24323-24329, Year 1993
Publish dateAug 9, 1993 (structure data deposition date)
AuthorsO'Brien, M.C. / McKay, D.B.
External linksPubMed:8226982
MethodsX-ray diffraction
Resolution2.34 - 2.43 Å
Structure data

PDB-1atr:
THREONINE 204 OF THE CHAPERONE PROTEIN HSC70 INFLUENCES THE STRUCTURE OF THE ACTIVE SITE BUT IS NOT ESSENTIAL FOR ATP HYDROLYSIS
Method: X-RAY DIFFRACTION / Resolution: 2.34 Å

PDB-1ats:
THREONINE 204 OF THE CHAPERONE PROTEIN HSC70 INFLUENCES THE STRUCTURE OF THE ACTIVE SITE BUT IS NOT ESSENTIAL FOR ATP HYDROLYSIS
Method: X-RAY DIFFRACTION / Resolution: 2.43 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-PO4:
PHOSPHATE ION / Phosphate

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-HOH:
WATER / Water

Source
  • bos taurus (cattle)
KeywordsCHAPERONE PROTEIN

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