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Atomistry » Potassium » PDB 4cn5-4edj » 4dgv | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Potassium » PDB 4cn5-4edj » 4dgv » |
Potassium in PDB 4dgv: Structure of the Hepatitis C Virus Envelope Glycoprotein E2 Antigenic Region 412-423 Bound to the Broadly Neutralizing Antibody HCV1, P2(1) FormProtein crystallography data
The structure of Structure of the Hepatitis C Virus Envelope Glycoprotein E2 Antigenic Region 412-423 Bound to the Broadly Neutralizing Antibody HCV1, P2(1) Form, PDB code: 4dgv
was solved by
L.Kong,
I.A.Wilson,
M.Law,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4dgv:
The structure of Structure of the Hepatitis C Virus Envelope Glycoprotein E2 Antigenic Region 412-423 Bound to the Broadly Neutralizing Antibody HCV1, P2(1) Form also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Structure of the Hepatitis C Virus Envelope Glycoprotein E2 Antigenic Region 412-423 Bound to the Broadly Neutralizing Antibody HCV1, P2(1) Form
(pdb code 4dgv). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total only one binding site of Potassium was determined in the Structure of the Hepatitis C Virus Envelope Glycoprotein E2 Antigenic Region 412-423 Bound to the Broadly Neutralizing Antibody HCV1, P2(1) Form, PDB code: 4dgv: Potassium binding site 1 out of 1 in 4dgvGo back to Potassium Binding Sites List in 4dgv
Potassium binding site 1 out
of 1 in the Structure of the Hepatitis C Virus Envelope Glycoprotein E2 Antigenic Region 412-423 Bound to the Broadly Neutralizing Antibody HCV1, P2(1) Form
Mono view Stereo pair view
Reference:
L.Kong,
E.Giang,
J.B.Robbins,
R.L.Stanfield,
D.R.Burton,
I.A.Wilson,
M.Law.
Structural Basis of Hepatitis C Virus Neutralization By Broadly Neutralizing Antibody HCV1. Proc.Natl.Acad.Sci.Usa V. 109 9499 2012.
Page generated: Sun Dec 13 23:30:03 2020
ISSN: ISSN 0027-8424 PubMed: 22623528 DOI: 10.1073/PNAS.1202924109 |
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