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Atomistry » Chlorine » PDB 5syw-5t6k » 5t1a » |
Chlorine in PDB 5t1a: Structure of Cc Chemokine Receptor 2 with Orthosteric and Allosteric AntagonistsEnzymatic activity of Structure of Cc Chemokine Receptor 2 with Orthosteric and Allosteric Antagonists
All present enzymatic activity of Structure of Cc Chemokine Receptor 2 with Orthosteric and Allosteric Antagonists:
3.2.1.17; Protein crystallography data
The structure of Structure of Cc Chemokine Receptor 2 with Orthosteric and Allosteric Antagonists, PDB code: 5t1a
was solved by
Y.Zheng,
L.Qin,
N.V.Ortiz Zacarias,
H.De Vries,
G.W.Han,
M.Gustavsson,
M.Dabros,
C.Zhao,
R.J.Cherney,
P.Carter,
D.Stamos,
R.Abagyan,
V.Cherezov,
R.C.Stevens,
A.P.Ijzerman,
L.H.Heitman,
A.Tebben,
I.Kufareva,
T.M.Handel,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5t1a:
The structure of Structure of Cc Chemokine Receptor 2 with Orthosteric and Allosteric Antagonists also contains other interesting chemical elements:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Structure of Cc Chemokine Receptor 2 with Orthosteric and Allosteric Antagonists
(pdb code 5t1a). 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 Structure of Cc Chemokine Receptor 2 with Orthosteric and Allosteric Antagonists, PDB code: 5t1a: Chlorine binding site 1 out of 1 in 5t1aGo back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Structure of Cc Chemokine Receptor 2 with Orthosteric and Allosteric Antagonists
![]() Mono view ![]() Stereo pair view
Reference:
Y.Zheng,
L.Qin,
N.V.Zacarias,
H.De Vries,
G.W.Han,
M.Gustavsson,
M.Dabros,
C.Zhao,
R.J.Cherney,
P.Carter,
D.Stamos,
R.Abagyan,
V.Cherezov,
R.C.Stevens,
A.P.Ijzerman,
L.H.Heitman,
A.Tebben,
I.Kufareva,
T.M.Handel.
Structure of Cc Chemokine Receptor 2 with Orthosteric and Allosteric Antagonists. Nature V. 540 458 2016.
Page generated: Sat Jul 12 08:46:23 2025
ISSN: ESSN 1476-4687 PubMed: 27926736 DOI: 10.1038/NATURE20605 |
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