Sodium in PDB 7sij: Myocilin Olf Mutant E352K

The structure of Myocilin Olf Mutant E352K, PDB code: 7sij was solved by H.S.Scelsi, B.M.Barlow, R.L.Lieberman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.26 / 1.54
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.336, 50.734, 50.49, 90, 96.6, 90
R / Rfree (%)	15.5 / 17.8

The structure of Myocilin Olf Mutant E352K also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Sodium atom in the Myocilin Olf Mutant E352K (pdb code 7sij). 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 Myocilin Olf Mutant E352K, PDB code: 7sij:

Sodium binding site 1 out of 1 in the Myocilin Olf Mutant E352K


Mono view


Stereo pair view

A full contact list of Sodium with other atoms in the Na binding site number 1 of Myocilin Olf Mutant E352K within 5.0Å range: probe atom residue distance (Å) B Occ A:Na1303 b:7.8 occ:1.00 O A:LEU381 2.3 7.8 1.0 OD1 A:ASP380 2.3 7.5 1.0 O A:HOH1435 2.4 7.6 1.0 OD2 A:ASP478 2.4 9.5 1.0 O A:GLY326 2.6 6.5 1.0 OD1 A:ASP478 2.8 7.6 1.0 CG A:ASP478 3.0 7.0 1.0 C A:GLY326 3.3 7.5 1.0 C A:LEU381 3.3 7.8 1.0 CG A:ASP380 3.5 8.4 1.0 N A:LEU381 3.5 6.1 1.0 O A:HOH1506 3.6 8.4 1.0 CA A:GLY326 3.6 7.2 1.0 O A:HOH1494 3.8 6.8 1.0 O A:ALA327 3.8 6.9 1.0 CG1 A:VAL328 3.8 7.5 1.0 CA A:CA1302 3.9 6.1 1.0 CA A:LEU381 3.9 8.0 1.0 C A:ASP380 4.1 8.9 1.0 O A:HOH1414 4.2 10.2 1.0 OD2 A:ASP380 4.3 8.1 1.0 N A:ALA327 4.3 6.2 1.0 C A:ALA327 4.3 5.8 1.0 CA A:ASP380 4.4 6.9 1.0 N A:ALA382 4.5 6.8 1.0 CB A:ASP478 4.5 5.2 1.0 CB A:LEU381 4.5 7.8 1.0 CB A:ASP380 4.6 6.7 1.0 O A:THR325 4.6 7.2 1.0 CA A:ALA382 4.8 6.6 1.0 CA A:ALA327 4.8 7.0 1.0 O A:HOH1555 4.9 10.0 1.0 O A:ASP380 4.9 8.8 1.0 N A:GLY326 4.9 7.5 1.0

H.F.Scelsi, K.R.Hill, B.M.Barlow, M.D.Martin, R.L.Lieberman. Disambiguation of Benign and Misfolded Glaucoma-Causing Myocilin Variants on the Basis of Protein Thermal Stability. Dis Model Mech 2022.
ISSN: ISSN 1754-8411
PubMed: 36579626
DOI: 10.1242/DMM.049816