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Ligands
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ADP Adenosine-5'-diphosphate
MG Magnesium ion
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Code : 1ATS   PDBj   RCSB PDB   PDBe
Header : CHAPERONE PROTEIN
Title : THREONINE 204 OF THE CHAPERONE PROTEIN HSC70 INFLUENCES THE STRUCTURE OF THE ACTIVE SITE BUT IS NOT ESSENTIAL FOR ATP HYDROLYSIS
Release Data : 1993-10-31
Compound :
mol_id molecule chains
1 HEAT-SHOCK COGNATE 70 KD PROTEIN A
ec: 3.6.1.3
Source :
mol_id organism_scientific organism_common
1 Bos taurus  (taxid:9913) Cattle
organ: BRAIN
Authors : O'Brien, M.C., Mckay, D.B.
Keywords : CHAPERONE PROTEIN
Exp. method : X-RAY DIFFRACTION ( 2.43 Å )
Citation :

Threonine 204 of the chaperone protein Hsc70 influences the structure of the active site, but is not essential for ATP hydrolysis.

O'Brien, M.C.,McKay, D.B.
(1993)  J.Biol.Chem.  268 : 24323 - 24329

PubMed: 8226982

Three-Dimensional Structure of the ATPase Fragment of a 70K Heat-Shock Cognate Protein

Flaherty, K.M.,De Luca-Flaherty, C.,Mckay, D.B.
(1990)  Nature  346 : 623

Chain : A
UniProt : P19120 (HSP7C_BOVIN)
Reaction: EC: Evidence:
Physiological Direction:
ATP + H2O = ADP + H(+) + phosphate 3.6.4.10 UniProtKB:P11142
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