Magnesium in PDB 2anx: Crystal Structure of Bacteriophage P22 Lysozyme Mutant L87M

All present enzymatic activity of Crystal Structure of Bacteriophage P22 Lysozyme Mutant L87M:
3.2.1.17;

The structure of Crystal Structure of Bacteriophage P22 Lysozyme Mutant L87M, PDB code: 2anx was solved by B.H.Mooers, B.W.Matthews, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.00 / 1.04
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	134.013, 50.415, 46.587, 90.00, 103.80, 90.00
R / Rfree (%)	11.7 / 15

The structure of Crystal Structure of Bacteriophage P22 Lysozyme Mutant L87M also contains other interesting chemical elements:

Samarium	(Sm)	3 atoms
Iodine	(I)	9 atoms

The binding sites of Magnesium atom in the Crystal Structure of Bacteriophage P22 Lysozyme Mutant L87M (pdb code 2anx). 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 Bacteriophage P22 Lysozyme Mutant L87M, PDB code: 2anx:

Magnesium binding site 1 out of 1 in the Crystal Structure of Bacteriophage P22 Lysozyme Mutant L87M


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 Bacteriophage P22 Lysozyme Mutant L87M within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg2831 b:8.0 occ:0.53 OD2 A:ASP69 1.9 26.4 1.0 CG A:ASP69 3.2 23.0 1.0 CA A:ASP69 3.9 15.5 1.0 OD1 A:ASP69 4.0 29.4 1.0 CB A:ASP69 4.1 19.1 1.0 N A:ASP69 4.2 13.5 1.0 O A:HOH3075 4.4 18.1 0.5 C A:GLU68 4.5 12.4 1.0 OG A:SER72 4.5 15.4 0.3 O A:HOH3200 4.6 38.1 1.0 O A:GLU68 4.7 13.6 1.0 O A:GLN65 4.8 13.3 1.0 CB A:GLU68 4.9 13.8 1.0 CG A:GLN65 5.0 20.6 1.0 O A:HOH4601 5.0 33.7 1.0 CB A:SER72 5.0 24.9 0.7

B.H.Mooers, B.W.Matthews. Extension to 2268 Atoms of Direct Methods in the Ab Initio Determination of the Unknown Structure of Bacteriophage P22 Lysozyme. Acta Crystallogr.,Sect.D V. 62 165 2006.
ISSN: ISSN 0907-4449
PubMed: 16421448
DOI: 10.1107/S0907444905037212