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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) Form

Protein 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:

Resolution Low / High (Å) 44.02 / 1.80
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 44.041, 75.301, 60.800, 90.00, 91.53, 90.00
R / Rfree (%) 17 / 21.4

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:

Sodium (Na) 1 atom

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 4dgv

Go 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

A full contact list of Potassium with other atoms in the K binding site number 1 of Structure of the Hepatitis C Virus Envelope Glycoprotein E2 Antigenic Region 412-423 Bound to the Broadly Neutralizing Antibody HCV1, P2(1) Form within 5.0Å range:
probe atom residue distance (Å) B Occ
H:K302

b:20.3
occ:1.00
N H:TYR59 3.4 16.4 1.0
NE H:ARG64 3.4 18.4 1.0
O H:TYR59 3.8 16.5 1.0
CA H:TYR58 3.9 15.1 1.0
CD1 H:TYR58 4.0 16.9 1.0
CD1 H:TYR59 4.0 14.8 1.0
NH2 H:ARG64 4.1 20.1 1.0
C H:TYR58 4.1 13.2 1.0
CB H:TYR59 4.2 13.8 1.0
CZ H:ARG64 4.2 26.6 1.0
CB H:TYR58 4.2 14.2 1.0
CD H:ARG64 4.2 21.3 1.0
CA H:TYR59 4.2 11.8 1.0
C H:TYR59 4.5 14.2 1.0
CH2 L:TRP94 4.5 21.4 1.0
CG H:ARG64 4.5 18.2 1.0
CG H:TYR58 4.6 16.3 1.0
CG H:TYR59 4.6 14.7 1.0
O H:LYS57 4.8 16.1 1.0
CE1 H:TYR58 4.9 19.8 1.0
CE1 H:TYR59 5.0 16.5 1.0

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.
ISSN: ISSN 0027-8424
PubMed: 22623528
DOI: 10.1073/PNAS.1202924109
Page generated: Mon Aug 12 10:32:03 2024

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