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Magnesium in PDB 7n37: Crystal Structure of 3-Site Deamidated Variant of Human Gamma(S)- Crystallin

Protein crystallography data

The structure of Crystal Structure of 3-Site Deamidated Variant of Human Gamma(S)- Crystallin, PDB code: 7n37 was solved by B.Norton-Baker, P.Mehrabi, R.W.Martin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.62 / 1.30
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 29.449, 62.552, 79.626, 90, 90, 90
R / Rfree (%) 14.5 / 17.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of 3-Site Deamidated Variant of Human Gamma(S)- Crystallin (pdb code 7n37). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of 3-Site Deamidated Variant of Human Gamma(S)- Crystallin, PDB code: 7n37:

Magnesium binding site 1 out of 1 in 7n37

Go back to Magnesium Binding Sites List in 7n37
Magnesium binding site 1 out of 1 in the Crystal Structure of 3-Site Deamidated Variant of Human Gamma(S)- Crystallin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of 3-Site Deamidated Variant of Human Gamma(S)- Crystallin within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg201

b:29.3
occ:0.89
O A:HOH361 2.1 32.8 1.0
O A:HOH303 2.2 34.4 1.0
O A:HOH444 2.5 45.8 1.0
O A:HOH301 3.6 56.1 1.0
OE1 A:GLU121 4.2 37.5 1.0
O A:HOH427 4.2 25.0 1.0
O A:ASP114 4.2 19.1 1.0
O A:HOH477 4.4 37.8 1.0
O A:HOH402 4.4 47.5 1.0
CD A:PRO116 4.4 19.2 1.0
O A:HOH476 4.5 42.0 1.0
CD A:GLU121 4.7 34.7 1.0
OE1 A:GLU113 5.0 46.6 1.0
OE2 A:GLU121 5.0 39.1 1.0

Reference:

B.Norton-Baker, P.Mehrabi, A.O.Kwok, K.W.Roskamp, M.A.Rocha, M.A.Sprague-Piercy, D.Von Stetten, R.J.D.Miller, R.W.Martin. Deamidation of the Human Eye Lens Protein Gamma S-Crystallin Accelerates Oxidative Aging. Structure V. 30 763 2022.
ISSN: ISSN 0969-2126
PubMed: 35338852
DOI: 10.1016/J.STR.2022.03.002
Page generated: Thu Apr 6 17:40:10 2023

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