Magnesium in PDB 2uag: Udp-N-Acetylmuramoyl-L-Alanine:D-Glutamate Ligase

All present enzymatic activity of Udp-N-Acetylmuramoyl-L-Alanine:D-Glutamate Ligase:
6.3.2.9;

The structure of Udp-N-Acetylmuramoyl-L-Alanine:D-Glutamate Ligase, PDB code: 2uag was solved by J.Bertrand, E.Fanchon, O.Dideberg, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	8.00 / 1.70
Space group	P 41
Cell size a, b, c (Å), α, β, γ (°)	65.560, 65.560, 136.010, 90.00, 90.00, 90.00
R / Rfree (%)	18 / 20.6

The binding sites of Magnesium atom in the Udp-N-Acetylmuramoyl-L-Alanine:D-Glutamate Ligase (pdb code 2uag). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Udp-N-Acetylmuramoyl-L-Alanine:D-Glutamate Ligase, PDB code: 2uag:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Udp-N-Acetylmuramoyl-L-Alanine:D-Glutamate Ligase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Udp-N-Acetylmuramoyl-L-Alanine:D-Glutamate Ligase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1000 b:4.7 occ:1.00 O20 A:UMA450 1.8 6.3 1.0 O A:HOH1255 2.1 6.1 1.0 O A:HOH1177 2.1 6.9 1.0 O A:HOH1096 2.1 5.4 1.0 NE2 A:HIS183 2.1 4.3 1.0 O A:HOH1173 2.2 5.8 1.0 C22 A:UMA450 2.8 8.1 1.0 CE1 A:HIS183 3.0 6.2 1.0 CD2 A:HIS183 3.3 4.7 1.0 O19 A:UMA450 3.3 8.5 1.0 OD2 A:ASP182 3.6 5.8 1.0 O A:HOH1241 4.0 5.4 1.0 O A:HOH1094 4.0 5.5 1.0 C21 A:UMA450 4.1 7.2 1.0 OQ1 A:KCX198 4.1 3.6 1.0 ND1 A:HIS183 4.2 5.2 1.0 C23 A:UMA450 4.3 6.5 1.0 O A:HOH1174 4.3 4.4 1.0 NZ A:LYS115 4.3 2.9 1.0 OQ2 A:KCX198 4.3 4.3 1.0 CG A:HIS183 4.3 4.7 1.0 CG A:ASP182 4.5 5.4 1.0 CX A:KCX198 4.7 3.8 1.0 OG1 A:THR321 4.8 10.1 1.0 NZ A:LYS348 4.9 4.4 1.0 OD1 A:ASP182 4.9 5.0 1.0

Magnesium binding site 2 out of 2 in the Udp-N-Acetylmuramoyl-L-Alanine:D-Glutamate Ligase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Udp-N-Acetylmuramoyl-L-Alanine:D-Glutamate Ligase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1001 b:7.9 occ:1.00 O1B A:ADP451 2.1 5.1 1.0 OG A:SER116 2.1 4.8 1.0 O A:HOH1310 2.1 5.3 1.0 O A:HOH1309 2.1 7.1 1.0 O A:HOH1126 2.2 5.0 1.0 OE2 A:GLU157 2.3 6.4 1.0 CD A:GLU157 3.2 5.8 1.0 PB A:ADP451 3.2 5.5 1.0 CB A:SER116 3.3 3.3 1.0 OE1 A:GLU157 3.4 6.5 1.0 O3B A:ADP451 3.5 5.1 1.0 N A:SER116 3.9 4.1 1.0 O1A A:ADP451 3.9 5.5 1.0 ND2 A:ASN138 4.1 4.6 1.0 CA A:SER116 4.1 4.0 1.0 O A:HOH1212 4.2 28.4 1.0 O A:HOH1311 4.2 25.4 1.0 O2B A:ADP451 4.2 4.0 1.0 O3A A:ADP451 4.3 6.0 1.0 NH2 A:ARG302 4.3 7.2 1.0 O A:ASN138 4.5 8.5 1.0 CG A:GLU157 4.5 4.5 1.0 PA A:ADP451 4.7 6.3 1.0 O A:HOH1313 4.7 15.7 1.0 CE A:LYS115 4.7 2.4 1.0 CB A:LYS115 4.7 3.2 1.0 CA A:ILE139 4.8 8.5 1.0 C A:LYS115 4.9 3.6 1.0 O19 A:UMA450 4.9 8.5 1.0 C A:ASN138 5.0 6.7 1.0

J.A.Bertrand, G.Auger, L.Martin, E.Fanchon, D.Blanot, D.Le Beller, J.Van Heijenoort, O.Dideberg. Determination of the Murd Mechanism Through Crystallographic Analysis of Enzyme Complexes. J.Mol.Biol. V. 289 579 1999.
ISSN: ISSN 0022-2836
PubMed: 10356330
DOI: 10.1006/JMBI.1999.2800