Magnesium in PDB 4grh: Crystal Structure of Pabb of Stenotrophomonas Maltophilia

All present enzymatic activity of Crystal Structure of Pabb of Stenotrophomonas Maltophilia:
2.6.1.85;

The structure of Crystal Structure of Pabb of Stenotrophomonas Maltophilia, PDB code: 4grh was solved by A.Bera, V.Atanasova, J.E.Ladner, J.F.Parsons, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.57 / 2.25
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	161.300, 161.300, 116.089, 90.00, 90.00, 120.00
R / Rfree (%)	19.4 / 24

The binding sites of Magnesium atom in the Crystal Structure of Pabb of Stenotrophomonas Maltophilia (pdb code 4grh). 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 Crystal Structure of Pabb of Stenotrophomonas Maltophilia, PDB code: 4grh:

Magnesium binding site 1 out of 1 in the Crystal Structure of Pabb of Stenotrophomonas Maltophilia


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 Pabb of Stenotrophomonas Maltophilia within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg507 b:52.7 occ:1.00 O A:HOH830 2.0 52.3 1.0 O A:HOH828 2.0 65.5 1.0 O A:HOH831 2.1 35.5 1.0 O A:HOH832 2.2 58.8 1.0 O A:HOH829 2.2 52.9 1.0 OD2 A:ASP284 2.3 63.5 1.0 CG A:ASP284 3.1 67.6 1.0 OD1 A:ASP284 3.3 59.2 1.0 O A:GLU331 4.1 32.8 0.5 OD2 A:ASP429 4.3 33.2 1.0 O A:GLU331 4.3 32.9 0.5 O A:GLY282 4.3 38.6 1.0 OE1 A:GLU281 4.3 48.9 1.0 OE2 A:GLU331 4.5 34.4 0.5 CB A:GLU281 4.5 37.6 1.0 CB A:ASP284 4.6 56.5 1.0 N A:ASP284 4.7 63.7 1.0 O A:HOH660 4.7 41.8 1.0 N A:GLY282 4.7 32.5 1.0 CD A:GLU281 4.8 50.1 1.0 C A:GLU331 4.9 32.0 0.5 C A:GLY282 4.9 43.3 1.0 C A:GLU331 4.9 32.0 0.5 CG A:GLU281 4.9 42.9 1.0 CG A:GLU331 4.9 34.3 0.5

A.K.Bera, V.Atanasova, A.Dhanda, J.E.Ladner, J.F.Parsons. Structure of Aminodeoxychorismate Synthase From Stenotrophomonas Maltophilia. Biochemistry V. 51 10208 2012.
ISSN: ISSN 0006-2960
PubMed: 23230967
DOI: 10.1021/BI301243V