Magnesium in PDB 2hgs: Human Glutathione Synthetase

All present enzymatic activity of Human Glutathione Synthetase:
6.3.2.3;

The structure of Human Glutathione Synthetase, PDB code: 2hgs was solved by G.Polekhina, P.Board, J.Rossjohn, M.W.Parker, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.10
Space group	P 41 2 2
Cell size a, b, c (Å), α, β, γ (°)	84.260, 84.260, 197.620, 90.00, 90.00, 90.00
R / Rfree (%)	21.8 / 28.1

The binding sites of Magnesium atom in the Human Glutathione Synthetase (pdb code 2hgs). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Human Glutathione Synthetase, PDB code: 2hgs:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Human Glutathione Synthetase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Human Glutathione Synthetase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg501 b:31.3 occ:1.00 O3B A:ADP500 1.9 35.1 1.0 OE2 A:GLU144 2.0 36.9 1.0 OE1 A:GLU368 2.1 38.4 1.0 O2 A:SO4505 2.1 30.4 1.0 OD1 A:ASN146 2.2 29.1 1.0 OE1 A:GLU144 2.4 29.9 1.0 CD A:GLU144 2.6 33.9 1.0 CD A:GLU368 3.1 39.0 1.0 PB A:ADP500 3.1 31.8 1.0 CG A:ASN146 3.2 24.2 1.0 S A:SO4505 3.3 30.7 1.0 O1B A:ADP500 3.3 30.9 1.0 O1 A:SO4505 3.5 33.7 1.0 OE2 A:GLU368 3.5 33.1 1.0 MG A:MG502 3.6 29.4 1.0 ND2 A:ASN146 3.7 24.2 1.0 N A:GLY369 3.8 30.0 1.0 O4 A:SO4505 3.9 30.2 1.0 NZ A:LYS305 3.9 21.9 1.0 O3A A:ADP500 3.9 32.2 1.0 CG A:GLU144 4.1 30.1 1.0 O A:HOH734 4.2 23.5 1.0 CA A:GLU368 4.2 33.1 1.0 O A:HOH553 4.3 30.5 1.0 O2B A:ADP500 4.3 26.8 1.0 CG A:GLU368 4.3 34.2 1.0 CB A:GLU368 4.4 31.0 1.0 O3 A:SO4505 4.5 32.4 1.0 O2A A:ADP500 4.5 29.9 1.0 CB A:ASN146 4.5 29.8 1.0 C A:GLU368 4.6 30.7 1.0 CE A:LYS305 4.7 28.8 1.0 PA A:ADP500 4.8 32.3 1.0 O A:HOH523 4.8 30.7 1.0 CA A:GLY369 4.9 31.8 1.0 CA A:ASN146 4.9 24.6 1.0 CB2 A:GSH503 4.9 30.8 1.0 CB A:GLU144 4.9 28.2 1.0 SG2 A:GSH503 5.0 33.2 1.0 O A:HOH735 5.0 28.3 1.0

Magnesium binding site 2 out of 2 in the Human Glutathione Synthetase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Human Glutathione Synthetase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:29.4 occ:1.00 O1B A:ADP500 2.1 30.9 1.0 O2A A:ADP500 2.1 29.9 1.0 O1 A:SO4505 2.1 33.7 1.0 O A:HOH735 2.2 28.3 1.0 OE2 A:GLU144 2.2 36.9 1.0 O A:HOH622 2.2 31.7 1.0 CD A:GLU144 3.1 33.9 1.0 PA A:ADP500 3.2 32.3 1.0 PB A:ADP500 3.3 31.8 1.0 S A:SO4505 3.4 30.7 1.0 O3A A:ADP500 3.5 32.2 1.0 CG A:GLU144 3.6 30.1 1.0 MG A:MG501 3.6 31.3 1.0 O A:HOH623 3.6 31.8 1.0 O2 A:SO4505 3.7 30.4 1.0 O3B A:ADP500 3.8 35.1 1.0 O3' A:ADP500 3.9 31.8 1.0 NH2 A:ARG450 4.0 27.1 1.0 OD2 A:ASP127 4.0 26.8 1.0 C5' A:ADP500 4.0 32.0 1.0 O5' A:ADP500 4.1 30.3 1.0 ND2 A:ASN146 4.1 24.2 1.0 OE1 A:GLU144 4.2 29.9 1.0 OE2 A:GLU425 4.2 32.1 1.0 NH1 A:ARG450 4.3 28.4 1.0 O3 A:SO4505 4.3 32.4 1.0 O4 A:SO4505 4.3 30.2 1.0 O1A A:ADP500 4.3 36.7 1.0 C3' A:ADP500 4.5 31.4 1.0 O2B A:ADP500 4.5 26.8 1.0 OD1 A:ASN146 4.6 29.1 1.0 CZ A:ARG450 4.6 32.0 1.0 C4' A:ADP500 4.7 30.8 1.0 CG A:ASN146 4.8 24.2 1.0 NH2 A:ARG125 4.9 27.0 1.0 CG2 A:ILE143 4.9 24.3 1.0 CG A:ASP127 4.9 33.3 1.0 CB A:GLU144 5.0 28.2 1.0

G.Polekhina, P.G.Board, R.R.Gali, J.Rossjohn, M.W.Parker. Molecular Basis of Glutathione Synthetase Deficiency and A Rare Gene Permutation Event. Embo J. V. 18 3204 1999.
ISSN: ISSN 0261-4189
PubMed: 10369661
DOI: 10.1093/EMBOJ/18.12.3204