Calcium in PDB 4wxu: Crystal Structure of the Selenomthionine Incorporated Myocilin Olfactomedin Domain E396D Variant.

The structure of Crystal Structure of the Selenomthionine Incorporated Myocilin Olfactomedin Domain E396D Variant., PDB code: 4wxu was solved by R.K.Donegan, D.M.Freeman, R.L.Lieberman, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.60 / 2.09
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	49.484, 50.560, 50.537, 90.00, 97.27, 90.00
R / Rfree (%)	17.8 / 20.1

The structure of Crystal Structure of the Selenomthionine Incorporated Myocilin Olfactomedin Domain E396D Variant. also contains other interesting chemical elements:

Sodium

(Na)

1 atom

The binding sites of Calcium atom in the Crystal Structure of the Selenomthionine Incorporated Myocilin Olfactomedin Domain E396D Variant. (pdb code 4wxu). 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 Crystal Structure of the Selenomthionine Incorporated Myocilin Olfactomedin Domain E396D Variant., PDB code: 4wxu:

Calcium binding site 1 out of 1 in the Crystal Structure of the Selenomthionine Incorporated Myocilin Olfactomedin Domain E396D Variant.


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of the Selenomthionine Incorporated Myocilin Olfactomedin Domain E396D Variant. within 5.0Å range: probe atom residue distance (Å) B Occ A:Ca601 b:12.5 occ:1.00 OD2 A:ASP380 2.4 6.2 1.0 O A:ILE477 2.4 5.0 1.0 O A:ALA429 2.4 4.2 1.0 OD1 A:ASP478 2.5 7.9 1.0 OD1 A:ASN428 2.5 1.8 1.0 O A:HOH889 2.6 4.1 1.0 O A:HOH851 2.7 6.0 1.0 CG A:ASP380 3.2 6.0 1.0 OD1 A:ASP380 3.2 7.0 1.0 H A:ALA429 3.4 8.4 1.0 C A:ILE477 3.5 5.8 1.0 HA A:ASP478 3.5 5.6 1.0 H A:ILE477 3.6 3.4 1.0 C A:ALA429 3.6 6.2 1.0 CG A:ASP478 3.7 6.8 1.0 CG A:ASN428 3.7 6.7 1.0 NA A:NA607 3.9 12.5 1.0 HB3 A:PHE430 3.9 7.6 1.0 HH A:TYR371 4.0 5.0 1.0 HD21 A:ASN428 4.1 4.4 1.0 HA A:PHE430 4.1 7.3 1.0 N A:ALA429 4.1 7.0 1.0 CA A:ASP478 4.2 4.6 1.0 N A:ASP478 4.2 5.7 1.0 N A:ILE477 4.3 2.8 1.0 ND2 A:ASN428 4.3 3.6 1.0 HB A:ILE477 4.4 7.7 1.0 CA A:ILE477 4.4 3.9 1.0 HE2 A:TYR371 4.5 5.9 1.0 OD2 A:ASP478 4.5 8.3 1.0 CA A:ALA429 4.5 6.7 1.0 HD12 A:ILE391 4.5 10.2 1.0 CB A:ASP478 4.5 7.3 1.0 OH A:TYR371 4.6 4.2 1.0 O A:HOH890 4.6 5.6 1.0 O A:HOH891 4.6 4.3 1.0 N A:PHE430 4.6 6.6 1.0 CB A:ASP380 4.6 7.0 1.0 HB3 A:ASN428 4.7 7.0 1.0 CA A:PHE430 4.7 6.1 1.0 O A:HOH930 4.7 4.0 1.0 CB A:PHE430 4.7 6.4 1.0 CB A:ASN428 4.8 5.8 1.0 HB3 A:ASP380 4.9 8.4 1.0 O A:LEU381 4.9 3.4 1.0 HD2 A:PHE430 4.9 6.5 1.0 HB2 A:ASP380 4.9 8.4 1.0 CB A:ILE477 5.0 6.4 1.0 HG2 A:MSE476 5.0 8.1 1.0 HB2 A:ASP478 5.0 8.8 1.0 HB3 A:ALA429 5.0 4.6 1.0 CE2 A:TYR371 5.0 4.9 1.0

R.K.Donegan, S.E.Hill, D.M.Freeman, E.Nguyen, S.D.Orwig, K.C.Turnage, R.L.Lieberman. Structural Basis For Misfolding in Myocilin-Associated Glaucoma. Hum.Mol.Genet. V. 24 2111 2015.
ISSN: ESSN 1460-2083
PubMed: 25524706
DOI: 10.1093/HMG/DDU730