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Sodium in PDB 7skd: Myocilin Olf Mutant S331L

Protein crystallography data

The structure of Myocilin Olf Mutant S331L, PDB code: 7skd 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) 35.13 / 1.71
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 49.18, 50.6, 50.28, 90, 97.15, 90
R / Rfree (%) 22.7 / 28.2

Other elements in 7skd:

The structure of Myocilin Olf Mutant S331L also contains other interesting chemical elements:

Calcium (Ca) 1 atom

Sodium Binding Sites:

The binding sites of Sodium atom in the Myocilin Olf Mutant S331L (pdb code 7skd). 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 S331L, PDB code: 7skd:

Sodium binding site 1 out of 1 in 7skd

Go back to Sodium Binding Sites List in 7skd
Sodium binding site 1 out of 1 in the Myocilin Olf Mutant S331L


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 S331L within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Na602

b:19.0
occ:1.00
OD1 A:ASP380 2.3 17.8 1.0
O A:LEU381 2.4 17.1 1.0
OD2 A:ASP478 2.4 19.0 1.0
O A:GLY326 2.5 13.0 1.0
OD1 A:ASP478 2.8 14.6 1.0
CG A:ASP478 3.0 21.5 1.0
C A:GLY326 3.2 16.5 1.0
C A:LEU381 3.4 18.5 1.0
N A:LEU381 3.5 14.3 1.0
CA A:GLY326 3.6 16.6 1.0
CG A:ASP380 3.6 26.2 1.0
O A:HOH732 3.6 13.8 1.0
CG1 A:VAL328 3.7 12.2 1.0
O A:ALA327 3.7 13.8 1.0
CA A:CA601 3.9 15.8 1.0
CA A:LEU381 4.0 14.0 1.0
C A:ASP380 4.1 17.2 1.0
O A:HOH706 4.1 22.9 1.0
N A:ALA327 4.3 18.1 1.0
OD2 A:ASP380 4.3 14.3 1.0
C A:ALA327 4.4 13.7 1.0
CA A:ASP380 4.4 16.8 1.0
CB A:ASP478 4.5 10.5 1.0
CB A:LEU381 4.5 18.2 1.0
O A:THR325 4.6 18.6 1.0
N A:ALA382 4.6 14.9 1.0
CB A:ASP380 4.6 15.1 1.0
CA A:ALA327 4.8 22.3 1.0
O A:ASP380 4.8 20.3 1.0
N A:GLY326 4.9 13.1 1.0
CA A:ALA382 4.9 20.9 1.0
O A:HOH770 5.0 13.6 1.0

Reference:

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
Page generated: Mon Aug 18 11:58:18 2025

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