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Sodium in PDB 5nzf: Complex of H275Y/I223V Mutant Variant of Neuraminidase From H1N1 Influenza Virus with Oseltamivir

Protein crystallography data

The structure of Complex of H275Y/I223V Mutant Variant of Neuraminidase From H1N1 Influenza Virus with Oseltamivir, PDB code: 5nzf was solved by P.Pachl, J.Pokorna, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 45.18 / 1.75
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 85.654, 127.217, 96.786, 90.00, 92.93, 90.00
R / Rfree (%) 21.4 / 25.5

Other elements in 5nzf:

The structure of Complex of H275Y/I223V Mutant Variant of Neuraminidase From H1N1 Influenza Virus with Oseltamivir also contains other interesting chemical elements:

Calcium (Ca) 9 atoms

Sodium Binding Sites:

The binding sites of Sodium atom in the Complex of H275Y/I223V Mutant Variant of Neuraminidase From H1N1 Influenza Virus with Oseltamivir (pdb code 5nzf). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total only one binding site of Sodium was determined in the Complex of H275Y/I223V Mutant Variant of Neuraminidase From H1N1 Influenza Virus with Oseltamivir, PDB code: 5nzf:

Sodium binding site 1 out of 1 in 5nzf

Go back to Sodium Binding Sites List in 5nzf
Sodium binding site 1 out of 1 in the Complex of H275Y/I223V Mutant Variant of Neuraminidase From H1N1 Influenza Virus with Oseltamivir


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Complex of H275Y/I223V Mutant Variant of Neuraminidase From H1N1 Influenza Virus with Oseltamivir within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Na514

b:21.2
occ:1.00
O D:HOH741 2.8 20.5 1.0
O D:HOH941 2.8 19.2 1.0
O D:ARG430 3.0 18.2 1.0
O D:GLY429 3.1 19.6 1.0
C D:ARG430 3.2 18.3 1.0
N D:PRO431 3.3 18.2 1.0
N D:LYS432 3.4 20.3 1.0
CD D:PRO431 3.4 19.1 1.0
C D:GLY429 3.8 17.9 1.0
CB D:LYS432 3.8 23.7 1.0
O D:HOH804 3.9 19.5 1.0
CG2 D:ILE427 4.0 13.8 1.0
CG D:LYS432 4.1 27.4 1.0
CA D:LYS432 4.1 22.0 1.0
O D:HOH806 4.2 16.7 1.0
CA D:ARG430 4.2 18.9 1.0
N D:ARG430 4.3 19.0 1.0
C D:PRO431 4.4 21.4 1.0
CA D:PRO431 4.4 20.2 1.0
N D:GLY429 4.4 13.7 1.0
O D:HOH742 4.4 22.8 1.0
C D:ARG428 4.6 13.5 1.0
CG D:PRO431 4.6 18.9 1.0
CA D:GLY429 4.7 15.4 1.0
O D:ILE427 4.7 15.8 1.0
N D:GLU433 4.7 18.5 1.0
CB D:ILE427 4.9 14.0 1.0
C D:LYS432 4.9 19.9 1.0
O D:ARG428 4.9 13.6 1.0
CA D:ARG428 4.9 12.9 1.0

Reference:

J.Pokorna, P.Pachl, E.Karlukova, J.Hejdanek, P.Rezacova, A.Machara, J.Hudlicky, J.Konvalinka, M.Kozisek. Kinetic, Thermodynamic, and Structural Analysis of Drug Resistance Mutations in Neuraminidase From the 2009 Pandemic Influenza Virus. Viruses V. 10 2018.
ISSN: ISSN 1999-4915
PubMed: 29933553
DOI: 10.3390/V10070339
Page generated: Mon Oct 7 23:04:48 2024

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