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Magnesium in PDB 8e8u: Structure of the Lor Domain of Human Aass

Enzymatic activity of Structure of the Lor Domain of Human Aass

All present enzymatic activity of Structure of the Lor Domain of Human Aass:
1.5.1.8; 1.5.1.9;

Protein crystallography data

The structure of Structure of the Lor Domain of Human Aass, PDB code: 8e8u was solved by S.Khamrui, M.B.Lazarus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 47.41 / 2.65
Space group P 1 21 1
Cell size a, b, c (Å), α, β, γ (°) 73.005, 131.944, 96.494, 90, 100.72, 90
R / Rfree (%) 27.8 / 31.9

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Structure of the Lor Domain of Human Aass (pdb code 8e8u). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Structure of the Lor Domain of Human Aass, PDB code: 8e8u:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in 8e8u

Go back to Magnesium Binding Sites List in 8e8u
Magnesium binding site 1 out of 2 in the Structure of the Lor Domain of Human Aass


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of the Lor Domain of Human Aass within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg501

b:25.6
occ:1.00
OD1 A:ASP388 3.8 46.4 1.0
O A:GLU373 4.0 33.0 1.0
OD2 A:ASP388 4.2 37.0 1.0
O D:GLU373 4.3 35.6 1.0
CG A:ASP388 4.4 38.6 1.0
OD1 D:ASP388 4.6 41.6 1.0
OD2 D:ASP388 4.6 41.2 1.0
CD2 A:HIS374 5.0 35.4 1.0

Magnesium binding site 2 out of 2 in 8e8u

Go back to Magnesium Binding Sites List in 8e8u
Magnesium binding site 2 out of 2 in the Structure of the Lor Domain of Human Aass


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Structure of the Lor Domain of Human Aass within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg501

b:32.5
occ:1.00
OD1 C:ASP388 4.1 41.9 1.0
O C:GLU373 4.2 21.2 1.0
O B:GLU373 4.3 15.6 1.0
OD1 B:ASP388 4.4 61.1 1.0
OD2 C:ASP388 4.4 36.2 1.0
OD2 B:ASP388 4.5 60.7 1.0
CG C:ASP388 4.7 35.5 1.0
CG B:ASP388 4.9 52.2 1.0

Reference:

J.Leandro, S.Khamrui, C.Suebsuwong, P.J.Chen, C.Secor, T.Dodatko, C.Yu, R.Sanchez, R.J.Devita, S.M.Houten, M.B.Lazarus. Characterization and Structure of the Human Lysine-2-Oxoglutarate Reductase Domain, A Novel Therapeutic Target For Treatment of Glutaric Aciduria Type 1. Open Biology V. 12 20179 2022.
ISSN: ESSN 2046-2441
PubMed: 36128717
DOI: 10.1098/RSOB.220179
Page generated: Fri Oct 4 01:06:06 2024

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