Magnesium in PDB 4maz: The Structure of Mall Mutant Enzyme V200S From Bacillus Subtilus

All present enzymatic activity of The Structure of Mall Mutant Enzyme V200S From Bacillus Subtilus:
3.2.1.10;

The structure of The Structure of Mall Mutant Enzyme V200S From Bacillus Subtilus, PDB code: 4maz was solved by J.K.Hobbs, W.Jiao, A.D.Easter, E.J.Parker, L.A.Schipper, V.L.Arcus, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.69 / 1.60
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	48.470, 100.710, 61.440, 90.00, 112.77, 90.00
R / Rfree (%)	16.1 / 18.8

The binding sites of Magnesium atom in the The Structure of Mall Mutant Enzyme V200S From Bacillus Subtilus (pdb code 4maz). 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 The Structure of Mall Mutant Enzyme V200S From Bacillus Subtilus, PDB code: 4maz:

Magnesium binding site 1 out of 1 in the The Structure of Mall Mutant Enzyme V200S From Bacillus Subtilus


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Structure of Mall Mutant Enzyme V200S From Bacillus Subtilus within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg604 b:3.3 occ:1.00 OD2 A:ASP28 2.2 10.6 1.0 OD1 A:ASP20 2.2 9.8 1.0 OD1 A:ASN22 2.3 12.2 1.0 O A:PHE26 2.3 8.2 1.0 O A:HOH867 2.3 10.5 1.0 OD1 A:ASP24 2.3 10.6 1.0 CG A:ASN22 3.2 13.0 1.0 CG A:ASP28 3.2 10.6 1.0 CG A:ASP24 3.3 11.2 1.0 CG A:ASP20 3.4 9.8 1.0 C A:PHE26 3.5 8.3 1.0 OD2 A:ASP24 3.7 12.3 1.0 ND2 A:ASN22 3.7 13.2 1.0 CB A:ASP28 3.7 9.7 1.0 N A:PHE26 4.1 9.0 1.0 N A:ASN22 4.1 11.8 1.0 OD2 A:ASP20 4.2 10.2 1.0 CA A:PHE26 4.2 8.7 1.0 CB A:ASP20 4.2 9.2 1.0 CA A:ASP20 4.3 9.1 1.0 N A:ASP24 4.3 11.8 1.0 OD1 A:ASP28 4.3 11.1 1.0 CB A:PHE26 4.4 9.0 1.0 N A:GLY23 4.4 12.4 1.0 CB A:ASN22 4.4 13.1 1.0 CB A:ASP24 4.5 11.9 1.0 O A:LYS73 4.5 10.5 1.0 C A:GLY27 4.5 8.4 1.0 N A:ASP28 4.5 8.6 1.0 N A:GLY27 4.5 8.1 1.0 CA A:ASN22 4.6 12.8 1.0 N A:ALA21 4.6 10.3 1.0 C A:ASP20 4.6 10.0 1.0 C A:ASN22 4.6 13.0 1.0 CA A:GLY27 4.6 8.1 1.0 CA A:ASP28 4.7 8.7 1.0 CA A:ASP24 4.8 11.8 1.0 N A:GLY25 4.8 10.6 1.0 O A:GLY27 4.8 8.1 1.0 C A:ASP24 4.9 11.1 1.0

J.K.Hobbs, W.Jiao, A.D.Easter, E.J.Parker, L.A.Schipper, V.L.Arcus. Change in Heat Capacity For Enzyme Catalysis Determines Temperature Dependence of Enzyme Catalyzed Rates. Acs Chem.Biol. V. 8 2388 2013.
ISSN: ISSN 1554-8929
PubMed: 24015933
DOI: 10.1021/CB4005029