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Calcium 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:

Sodium (Na) 1 atom

Calcium Binding Sites:

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

Calcium binding site 1 out of 1 in 7skd

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


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 S331L within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Ca601

b:15.8
occ:1.00
OD2 A:ASP380 2.4 14.3 1.0
O A:ALA429 2.4 11.7 1.0
OD1 A:ASP478 2.4 14.6 1.0
O A:ILE477 2.4 10.6 1.0
O A:HOH732 2.5 13.8 1.0
OD1 A:ASN428 2.6 16.4 1.0
OD1 A:ASP380 3.1 17.8 1.0
CG A:ASP380 3.1 26.2 1.0
C A:ILE477 3.5 14.4 1.0
C A:ALA429 3.6 20.9 1.0
CG A:ASP478 3.6 21.5 1.0
CG A:ASN428 3.7 14.7 1.0
NA A:NA602 3.9 19.0 1.0
N A:ALA429 4.1 17.4 1.0
CA A:ASP478 4.2 10.2 1.0
N A:ASP478 4.2 11.9 1.0
O A:HOH770 4.4 13.6 1.0
ND2 A:ASN428 4.4 13.5 1.0
OD2 A:ASP478 4.4 19.0 1.0
N A:ILE477 4.4 15.7 1.0
CA A:ALA429 4.5 18.4 1.0
CB A:ASP478 4.5 10.5 1.0
OH A:TYR371 4.5 19.2 1.0
CA A:ILE477 4.5 13.4 1.0
CB A:ASP380 4.5 15.1 1.0
N A:PHE430 4.5 13.8 1.0
CA A:PHE430 4.7 17.6 1.0
CB A:PHE430 4.8 13.3 1.0
CB A:ASN428 4.8 16.4 1.0
O A:LEU381 4.8 17.1 1.0
CE2 A:TYR371 4.9 15.0 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: Fri Jul 19 04:06:02 2024

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