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Atomistry » Magnesium » PDB 5ac0-5avx » 5aqu » |
Magnesium in PDB 5aqu: Fragment-Based Screening of HSP70 Sheds Light on the Functional Role of Atp-Binding Site ResiduesEnzymatic activity of Fragment-Based Screening of HSP70 Sheds Light on the Functional Role of Atp-Binding Site Residues
All present enzymatic activity of Fragment-Based Screening of HSP70 Sheds Light on the Functional Role of Atp-Binding Site Residues:
3.6.3.51; Protein crystallography data
The structure of Fragment-Based Screening of HSP70 Sheds Light on the Functional Role of Atp-Binding Site Residues, PDB code: 5aqu
was solved by
A.M.Jones,
I.M.Westwood,
J.D.Osborne,
T.P.Matthews,
M.D.Cheeseman,
M.G.Rowlands,
F.Jeganathan,
R.Burke,
D.Lee,
N.Kadi,
M.Liu,
M.Richards,
C.Mcandrew,
N.Yahya,
S.E.Dobson,
K.Jones,
P.Workman,
I.Collins,
R.L.M.Vanmontfort,
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 Fragment-Based Screening of HSP70 Sheds Light on the Functional Role of Atp-Binding Site Residues
(pdb code 5aqu). 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 Fragment-Based Screening of HSP70 Sheds Light on the Functional Role of Atp-Binding Site Residues, PDB code: 5aqu: Magnesium binding site 1 out of 1 in 5aquGo back to Magnesium Binding Sites List in 5aqu
Magnesium binding site 1 out
of 1 in the Fragment-Based Screening of HSP70 Sheds Light on the Functional Role of Atp-Binding Site Residues
Mono view Stereo pair view
Reference:
A.M.Jones,
I.M.Westwood,
J.D.Osborne,
T.P.Matthews,
M.D.Cheeseman,
M.G.Rowlands,
F.Jeganathan,
R.Burke,
D.Lee,
N.Kadi,
M.Liu,
M.Richards,
C.Mcandrew,
N.Yahya,
S.E.Dobson,
K.Jones,
P.Workman,
I.Collins,
R.L.Van Montfort.
A Fragment-Based Approach Applied to A Highly Flexible Target: Insights and Challenges Towards the Inhibition of HSP70 Isoforms. Sci Rep V. 6 34701 2016.
Page generated: Mon Dec 14 20:01:00 2020
ISSN: ESSN 2045-2322 PubMed: 27708405 DOI: 10.1038/SREP34701 |
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