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Atomistry » Chlorine » PDB 5mge-5mlr » 5ml9 » |
Chlorine in PDB 5ml9: Cocrystal Structure of Fc Gamma Receptor Iiia Interacting with Affimer F4, A Specific Binding Protein Which Blocks Igg Binding to the Receptor.Protein crystallography data
The structure of Cocrystal Structure of Fc Gamma Receptor Iiia Interacting with Affimer F4, A Specific Binding Protein Which Blocks Igg Binding to the Receptor., PDB code: 5ml9
was solved by
J.I.Robinson,
D.C.Tomlinson,
E.W.Baxter,
R.L.Owen,
M.Thomsen,
S.J.Win,
J.E.Nettleship,
C.Tiede,
R.J.Foster,
M.P.Waterhouse,
S.A.Harris,
R.J.Owens,
C.W.G.Fishwick,
A.Goldman,
M.J.Mcpherson,
A.W.Morgan,
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 Cocrystal Structure of Fc Gamma Receptor Iiia Interacting with Affimer F4, A Specific Binding Protein Which Blocks Igg Binding to the Receptor.
(pdb code 5ml9). 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 Cocrystal Structure of Fc Gamma Receptor Iiia Interacting with Affimer F4, A Specific Binding Protein Which Blocks Igg Binding to the Receptor., PDB code: 5ml9: Chlorine binding site 1 out of 1 in 5ml9Go back to Chlorine Binding Sites List in 5ml9
Chlorine binding site 1 out
of 1 in the Cocrystal Structure of Fc Gamma Receptor Iiia Interacting with Affimer F4, A Specific Binding Protein Which Blocks Igg Binding to the Receptor.
Mono view Stereo pair view
Reference:
J.I.Robinson,
E.W.Baxter,
R.L.Owen,
M.Thomsen,
D.C.Tomlinson,
M.P.Waterhouse,
S.J.Win,
J.E.Nettleship,
C.Tiede,
R.J.Foster,
R.J.Owens,
C.W.G.Fishwick,
S.A.Harris,
A.Goldman,
M.J.Mcpherson,
A.W.Morgan.
Affimer Proteins Inhibit Immune Complex Binding to Fc Gamma Riiia with High Specificity Through Competitive and Allosteric Modes of Action. Proc. Natl. Acad. Sci. V. 115 E72 2018U.S.A..
Page generated: Fri Jul 26 12:47:43 2024
ISSN: ESSN 1091-6490 PubMed: 29247053 DOI: 10.1073/PNAS.1707856115 |
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