Sodium in PDB 4p2z: Structure of Navms T207A/F214A

The structure of Structure of Navms T207A/F214A, PDB code: 4p2z was solved by C.Bagneris, C.E.Naylor, B.A.Wallace, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.68 / 3.08
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	80.010, 333.040, 80.390, 90.00, 90.00, 90.00
R / Rfree (%)	25.8 / 28.1

The binding sites of Sodium atom in the Structure of Navms T207A/F214A (pdb code 4p2z). This binding sites where shown within 5.0 Angstroms radius around Sodium atom.
In total 3 binding sites of Sodium where determined in the Structure of Navms T207A/F214A, PDB code: 4p2z:
Jump to Sodium binding site number: 1; 2; 3;

Sodium binding site 1 out of 3 in the Structure of Navms T207A/F214A


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Structure of Navms T207A/F214A within 5.0Å range:

Sodium binding site 2 out of 3 in the Structure of Navms T207A/F214A


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 2 of Structure of Navms T207A/F214A within 5.0Å range: probe atom residue distance (Å) B Occ C:Na302 b:0.2 occ:0.50 NA C:NA303 4.5 36.1 0.5

Sodium binding site 3 out of 3 in the Structure of Navms T207A/F214A


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 3 of Structure of Navms T207A/F214A within 5.0Å range: probe atom residue distance (Å) B Occ C:Na303 b:36.1 occ:0.50 NA C:NA302 4.5 0.2 0.5 OE2 C:GLU178 4.5 92.7 1.0 N C:SER179 4.6 46.1 1.0 N D:SER179 4.7 39.3 1.0 OE2 D:GLU178 4.7 62.8 1.0 CA C:GLU178 4.9 42.3 1.0 CA D:GLU178 5.0 33.7 1.0

C.Bagneris, P.G.Decaen, C.E.Naylor, D.C.Pryde, I.Nobeli, D.E.Clapham, B.A.Wallace. Prokaryotic Navms Channel As A Structural and Functional Model For Eukaryotic Sodium Channel Antagonism. Proc.Natl.Acad.Sci.Usa V. 111 8428 2014.
ISSN: ESSN 1091-6490
PubMed: 24850863
DOI: 10.1073/PNAS.1406855111