Magnesium in PDB 1hw6: Crystal Structure of Apo-2,5-Diketo-D-Gluconate Reductase

The structure of Crystal Structure of Apo-2,5-Diketo-D-Gluconate Reductase, PDB code: 1hw6 was solved by G.Sanli, M.Blaber, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.00 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	53.030, 53.940, 89.750, 90.00, 90.00, 90.00
R / Rfree (%)	20 / 26.8

The structure of Crystal Structure of Apo-2,5-Diketo-D-Gluconate Reductase also contains other interesting chemical elements:

Chlorine

(Cl)

2 atoms

The binding sites of Magnesium atom in the Crystal Structure of Apo-2,5-Diketo-D-Gluconate Reductase (pdb code 1hw6). 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 Apo-2,5-Diketo-D-Gluconate Reductase, PDB code: 1hw6:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Apo-2,5-Diketo-D-Gluconate 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 Apo-2,5-Diketo-D-Gluconate Reductase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg300 b:18.2 occ:1.00 O A:HOH507 1.9 19.2 1.0 O A:HOH504 2.0 17.8 1.0 O A:HOH456 2.1 15.3 1.0 OD2 A:ASP252 2.2 14.7 1.0 O A:HOH470 2.4 13.6 1.0 CG A:ASP252 3.2 17.6 1.0 OD1 A:ASP252 3.5 17.9 1.0 O A:HOH511 4.2 27.4 1.0 O A:HOH445 4.4 16.2 1.0 CB A:ASP252 4.5 7.0 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Apo-2,5-Diketo-D-Gluconate 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 Apo-2,5-Diketo-D-Gluconate Reductase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:28.1 occ:1.00 O A:HOH577 1.8 35.0 1.0 O A:HOH623 2.0 45.0 1.0 O A:HOH561 2.0 24.9 1.0 NE2 A:HIS180 2.2 14.5 1.0 O A:HOH619 2.4 37.3 1.0 CE1 A:HIS180 3.1 13.7 1.0 CD2 A:HIS180 3.3 14.3 1.0 OE2 A:GLU147 4.2 24.6 1.0 ND1 A:HIS180 4.3 13.7 1.0 CG A:HIS180 4.4 11.8 1.0 OE1 A:GLU147 4.8 17.9 1.0 CD A:GLU147 4.9 22.1 1.0 NE1 A:TRP176 4.9 18.8 1.0

G.Sanli, M.Blaber. Structural Assembly of the Active Site in An Aldo-Keto Reductase By Nadph Cofactor. J.Mol.Biol. V. 309 1209 2001.
ISSN: ISSN 0022-2836
PubMed: 11399090
DOI: 10.1006/JMBI.2001.4739