Sodium in PDB 2h6v: Spectroscopic and Structural Study of the Heterotropic Linkage Between Halide and Proton Ion Binding to Gfp Proteins- E2(Gfp) Apo Form

The structure of Spectroscopic and Structural Study of the Heterotropic Linkage Between Halide and Proton Ion Binding to Gfp Proteins- E2(Gfp) Apo Form, PDB code: 2h6v was solved by G.Garau, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.62 / 1.47
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	51.133, 62.850, 69.631, 90.00, 90.00, 90.00
R / Rfree (%)	15.9 / 18.7

The binding sites of Sodium atom in the Spectroscopic and Structural Study of the Heterotropic Linkage Between Halide and Proton Ion Binding to Gfp Proteins- E2(Gfp) Apo Form (pdb code 2h6v). 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 Spectroscopic and Structural Study of the Heterotropic Linkage Between Halide and Proton Ion Binding to Gfp Proteins- E2(Gfp) Apo Form, PDB code: 2h6v:

Sodium binding site 1 out of 1 in the Spectroscopic and Structural Study of the Heterotropic Linkage Between Halide and Proton Ion Binding to Gfp Proteins- E2(Gfp) Apo Form


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Spectroscopic and Structural Study of the Heterotropic Linkage Between Halide and Proton Ion Binding to Gfp Proteins- E2(Gfp) Apo Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1240 b:16.7 occ:1.00 O A:HOH1478 2.0 30.3 1.0 O A:HOH1495 2.1 31.0 1.0 OD2 A:ASP1197 2.1 17.5 1.0 O A:HOH1477 2.4 29.2 1.0 OD1 A:ASP1197 2.7 17.3 1.0 CG A:ASP1197 2.7 13.9 1.0 O A:HOH1473 3.9 24.8 1.0 CB A:ASP1197 4.1 11.5 1.0 O A:HOH1475 4.7 26.0 1.0

D.Arosio, G.Garau, F.Ricci, L.Marchetti, R.Bizzarri, R.Nifosi, F.Beltram. Spectroscopic and Structural Study of Proton and Halide Ion Cooperative Binding to Gfp Biophys.J. V. 93 232 2007.
ISSN: ISSN 0006-3495
PubMed: 17434942
DOI: 10.1529/BIOPHYSJ.106.102319