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Atomistry » Chlorine » PDB 5aoa-5b1k » 5aqn » |
Chlorine in PDB 5aqn: 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: 5aqn
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:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Fragment-Based Screening of HSP70 Sheds Light on the Functional Role of Atp-Binding Site Residues
(pdb code 5aqn). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Fragment-Based Screening of HSP70 Sheds Light on the Functional Role of Atp-Binding Site Residues, PDB code: 5aqn: Chlorine binding site 1 out of 1 in 5aqnGo back to![]() ![]()
Chlorine 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: Fri Jul 26 05:24:00 2024
ISSN: ESSN 2045-2322 PubMed: 27708405 DOI: 10.1038/SREP34701 |
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