Calcium in PDB 7sjv: Myocilin Olf Mutant T353I

The structure of Myocilin Olf Mutant T353I, PDB code: 7sjv 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)	35.24 / 1.39
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.365, 50.702, 50.644, 90, 96.85, 90
R / Rfree (%)	17.3 / 18.9

The structure of Myocilin Olf Mutant T353I also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Calcium atom in the Myocilin Olf Mutant T353I (pdb code 7sjv). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total only one binding site of Calcium was determined in the Myocilin Olf Mutant T353I, PDB code: 7sjv:

Calcium binding site 1 out of 1 in the Myocilin Olf Mutant T353I


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Myocilin Olf Mutant T353I within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca601 b:4.1 occ:1.00 OD2 A:ASP380 2.3 6.3 1.0 OD1 A:ASP478 2.3 5.6 1.0 O A:ALA429 2.4 4.0 1.0 O A:ILE477 2.4 4.1 1.0 O A:HOH770 2.4 4.3 1.0 OD1 A:ASN428 2.5 5.3 1.0 O A:HOH785 2.5 6.2 1.0 OD1 A:ASP380 3.0 5.5 1.0 CG A:ASP380 3.0 5.0 1.0 C A:ILE477 3.5 3.9 1.0 CG A:ASP478 3.6 6.0 1.0 C A:ALA429 3.6 2.9 1.0 CG A:ASN428 3.6 3.4 1.0 NA A:NA602 3.9 5.7 1.0 N A:ALA429 4.1 3.2 1.0 CA A:ASP478 4.2 4.1 1.0 N A:ASP478 4.2 3.4 1.0 ND2 A:ASN428 4.3 4.0 1.0 N A:ILE477 4.3 3.3 1.0 OD2 A:ASP478 4.4 7.9 1.0 O A:HOH723 4.5 5.0 1.0 CB A:ASP478 4.5 5.7 1.0 CA A:ILE477 4.5 3.6 1.0 OH A:TYR371 4.5 5.9 1.0 CA A:ALA429 4.5 4.4 1.0 O A:HOH813 4.5 7.9 1.0 O A:HOH791 4.5 4.9 1.0 CB A:ASP380 4.5 4.5 1.0 N A:PHE430 4.5 4.5 1.0 CA A:PHE430 4.6 3.8 1.0 CB A:PHE430 4.6 4.6 1.0 CB A:ASN428 4.7 4.7 1.0 O A:LEU381 4.8 5.2 1.0 CE2 A:TYR371 4.9 4.5 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