Magnesium in PDB 2wwr: Crystal Structure of Human Glyoxylate Reductase Hydroxypyruvate Reductase

All present enzymatic activity of Crystal Structure of Human Glyoxylate Reductase Hydroxypyruvate Reductase:
1.1.1.79;

The structure of Crystal Structure of Human Glyoxylate Reductase Hydroxypyruvate Reductase, PDB code: 2wwr was solved by M.P.S.Booth, R.Conners, G.Rumsby, R.L.Brady, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	100.00 / 2.82
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	67.356, 116.080, 198.230, 90.00, 90.00, 90.00
R / Rfree (%)	21.739 / 27.857

The binding sites of Magnesium atom in the Crystal Structure of Human Glyoxylate Reductase Hydroxypyruvate Reductase (pdb code 2wwr). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Human Glyoxylate Reductase Hydroxypyruvate Reductase, PDB code: 2wwr:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Human Glyoxylate Reductase Hydroxypyruvate Reductase


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 Human Glyoxylate Reductase Hydroxypyruvate Reductase within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1328 b:54.8 occ:1.00 OD1 B:ASP253 2.2 26.3 1.0 CG B:ASP253 3.4 24.9 1.0 OD2 C:ASP37 3.7 39.3 1.0 OD2 B:ASP253 4.0 24.5 1.0 OD1 C:ASP37 4.1 41.6 1.0 NZ D:LYS142 4.1 33.8 1.0 CG C:ASP37 4.3 40.1 1.0 OD1 B:ASN250 4.5 27.6 1.0 N B:ASP253 4.5 24.9 1.0 OE2 C:GLU38 4.5 38.0 1.0 CA B:ASP253 4.6 24.7 1.0 CB B:ASP253 4.6 24.9 1.0 CB B:ASP252 4.7 25.3 1.0 C B:ASP252 5.0 25.2 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Human Glyoxylate Reductase Hydroxypyruvate Reductase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of Human Glyoxylate Reductase Hydroxypyruvate Reductase within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg1328 b:50.5 occ:1.00 OD2 A:ASP37 3.6 29.2 1.0 OD1 A:ASP37 4.0 32.6 1.0 CG A:ASP37 4.2 30.4 1.0 OE2 A:GLU38 4.5 28.0 1.0 CE B:LYS142 4.8 26.4 1.0 NZ B:LYS142 4.8 24.4 1.0

M.P.Booth, R.Conners, G.Rumsby, R.L.Brady. Structural Basis of Substrate Specificity in Human Glyoxylate Reductase/Hydroxypyruvate Reductase. J.Mol.Biol. V. 360 178 2006.
ISSN: ISSN 0022-2836
PubMed: 16756993
DOI: 10.1016/J.JMB.2006.05.018