Magnesium in PDB 4knr: Hin Glmu Bound to WG188

All present enzymatic activity of Hin Glmu Bound to WG188:
2.3.1.157; 2.7.7.23;

The structure of Hin Glmu Bound to WG188, PDB code: 4knr was solved by P.Doig, S.L.Kazmirski, P.A.Boriack-Sjodin, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.00 / 2.10
Space group	H 3 2
Cell size a, b, c (Å), α, β, γ (°)	109.345, 109.345, 328.048, 90.00, 90.00, 120.00
R / Rfree (%)	21.6 / 24.9

The binding sites of Magnesium atom in the Hin Glmu Bound to WG188 (pdb code 4knr). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Hin Glmu Bound to WG188, PDB code: 4knr:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Hin Glmu Bound to WG188


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Hin Glmu Bound to WG188 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg504 b:48.5 occ:0.33 OD2 A:ASP406 2.1 51.9 1.0 O A:HOH605 2.1 47.0 1.0 CG A:ASP406 3.1 51.5 1.0 OD1 A:ASP406 3.5 50.4 1.0 NE2 A:GLN408 3.9 55.6 1.0 O A:ASP406 4.1 52.5 1.0 MG A:MG505 4.1 47.3 0.3 CB A:ASP406 4.3 51.9 1.0 O A:HOH631 4.9 52.5 1.0 C A:ASP406 5.0 51.6 1.0

Magnesium binding site 2 out of 2 in the Hin Glmu Bound to WG188


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Hin Glmu Bound to WG188 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg505 b:47.3 occ:0.33 OD1 A:ASP406 2.2 50.4 1.0 O A:HOH994 2.2 44.6 1.0 CG A:ASP406 3.2 51.5 1.0 OD2 A:ASP406 3.6 51.9 1.0 MG A:MG504 4.1 48.5 0.3 O A:HOH660 4.3 52.1 1.0 O A:GLY381 4.4 49.1 1.0 O A:HOH631 4.4 52.5 1.0 CB A:ASP406 4.5 51.9 1.0 CA A:ASP406 5.0 51.6 1.0 CA A:GLY381 5.0 49.4 1.0

P.Doig, P.A.Boriack-Sjodin, J.Dumas, J.Hu, K.Itoh, K.Johnson, S.Kazmirski, T.Kinoshita, S.Kuroda, T.O.Sato, K.Sugimoto, K.Tohyama, H.Aoi, K.Wakamatsu, H.Wang. Rational Design of Inhibitors of the Bacterial Cell Wall Synthetic Enzyme Glmu Using Virtual Screening and Lead-Hopping. Bioorg.Med.Chem. 2014.
ISSN: ESSN 1464-3391
PubMed: 25262942
DOI: 10.1016/J.BMC.2014.08.017