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Magnesium in PDB 1atr: Threonine 204 of the Chaperone Protein HSC70 Influences the Structure of the Active Site But Is Not Essential For Atp HydrolysisEnzymatic activity of Threonine 204 of the Chaperone Protein HSC70 Influences the Structure of the Active Site But Is Not Essential For Atp Hydrolysis
All present enzymatic activity of Threonine 204 of the Chaperone Protein HSC70 Influences the Structure of the Active Site But Is Not Essential For Atp Hydrolysis:
3.6.1.3; Protein crystallography data
The structure of Threonine 204 of the Chaperone Protein HSC70 Influences the Structure of the Active Site But Is Not Essential For Atp Hydrolysis, PDB code: 1atr
was solved by
M.C.O'brien,
D.B.Mckay,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Threonine 204 of the Chaperone Protein HSC70 Influences the Structure of the Active Site But Is Not Essential For Atp Hydrolysis
(pdb code 1atr). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Threonine 204 of the Chaperone Protein HSC70 Influences the Structure of the Active Site But Is Not Essential For Atp Hydrolysis, PDB code: 1atr: Magnesium binding site 1 out of 1 in 1atrGo back to Magnesium Binding Sites List in 1atr
Magnesium binding site 1 out
of 1 in the Threonine 204 of the Chaperone Protein HSC70 Influences the Structure of the Active Site But Is Not Essential For Atp Hydrolysis
Mono view Stereo pair view
Reference:
M.C.O'brien,
D.B.Mckay.
Threonine 204 of the Chaperone Protein HSC70 Influences the Structure of the Active Site, But Is Not Essential For Atp Hydrolysis. J.Biol.Chem. V. 268 24323 1993.
Page generated: Mon Dec 14 03:38:45 2020
ISSN: ISSN 0021-9258 PubMed: 8226982 |
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