Magnesium in PDB 9g5f: The Structure of Aspergillus Fumigatus Udp-Glcnac Pyrophosphorylase in Complex with A Fragment

All present enzymatic activity of The Structure of Aspergillus Fumigatus Udp-Glcnac Pyrophosphorylase in Complex with A Fragment:
2.7.7.23;

The structure of The Structure of Aspergillus Fumigatus Udp-Glcnac Pyrophosphorylase in Complex with A Fragment, PDB code: 9g5f was solved by K.Yan, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	52.33 / 1.62
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	56.43, 139.78, 144.19, 90, 90.04, 90
R / Rfree (%)	20.9 / 24.7

The binding sites of Magnesium atom in the The Structure of Aspergillus Fumigatus Udp-Glcnac Pyrophosphorylase in Complex with A Fragment (pdb code 9g5f). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the The Structure of Aspergillus Fumigatus Udp-Glcnac Pyrophosphorylase in Complex with A Fragment, PDB code: 9g5f:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the The Structure of Aspergillus Fumigatus Udp-Glcnac Pyrophosphorylase in Complex with A Fragment


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 Aspergillus Fumigatus Udp-Glcnac Pyrophosphorylase in Complex with A Fragment within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg604 b:48.0 occ:1.00 O B:VAL217 2.3 34.4 1.0 O B:HOH781 2.3 51.4 1.0 O B:LYS214 2.5 30.6 1.0 O D:HOH709 2.5 47.7 1.0 O B:HOH944 2.5 40.5 1.0 C B:VAL217 3.5 34.2 1.0 C B:LYS214 3.6 32.1 1.0 O B:HOH912 3.7 42.2 1.0 OD2 D:ASP347 3.9 56.8 1.0 CG B:LYS214 4.0 50.7 1.0 N B:VAL217 4.2 29.6 1.0 CA B:SER215 4.3 31.0 1.0 CA B:ILE218 4.3 29.3 1.0 N B:ILE218 4.4 28.5 1.0 N B:SER215 4.4 27.8 1.0 CA B:VAL217 4.4 29.0 1.0 C B:SER215 4.5 29.3 1.0 CA B:LYS214 4.5 36.3 1.0 CG1 B:ILE218 4.6 36.8 1.0 CD1 B:ILE218 4.7 37.5 1.0 CG D:ASP347 4.7 55.3 1.0 OH B:TYR209 4.7 39.4 1.0 CB D:ASP347 4.8 51.4 1.0 O B:SER215 4.8 28.7 1.0 CB B:LYS214 4.9 41.7 1.0 CB B:VAL217 4.9 31.3 1.0 N B:ASP216 4.9 26.3 1.0 CE2 B:TYR209 4.9 33.5 1.0

Magnesium binding site 2 out of 2 in the The Structure of Aspergillus Fumigatus Udp-Glcnac Pyrophosphorylase in Complex with A Fragment


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of The Structure of Aspergillus Fumigatus Udp-Glcnac Pyrophosphorylase in Complex with A Fragment within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg602 b:42.0 occ:1.00 O D:HOH859 2.3 45.6 1.0 O D:ASP99 2.3 34.0 1.0 OD1 D:ASP99 2.4 38.7 0.5 OG1 D:THR102 2.4 32.2 1.0 O D:THR102 2.5 33.7 1.0 O D:HOH874 3.1 53.3 1.0 C D:ASP99 3.2 36.9 1.0 C D:THR102 3.3 36.5 1.0 CG D:ASP99 3.3 35.7 0.5 CA D:ASP99 3.5 36.5 0.5 CA D:ASP99 3.5 38.1 0.5 CB D:THR102 3.6 31.8 1.0 CA D:THR102 3.8 35.1 1.0 CB D:ASP99 3.9 43.1 0.5 CB D:ASP99 3.9 39.0 0.5 N D:THR102 4.0 33.2 1.0 OD2 D:ASP99 4.0 48.4 0.5 OD2 D:ASP99 4.2 37.0 0.5 N D:ALA103 4.2 32.7 1.0 CG D:ASP99 4.3 42.8 0.5 N D:ILE100 4.5 38.2 1.0 CA D:ALA103 4.6 31.7 1.0 CG2 D:THR102 4.8 32.3 1.0 N D:ASP99 4.8 35.1 1.0 O D:HOH704 4.9 36.8 1.0 O D:PRO98 5.0 35.0 1.0

K.Yan, M.Stanley, O.Raimi, B.Kowalski, D.Gurvic, S.Grillenberger, X.Chen, A.T.Ferenbach, H.Dorfmueller, D.M.F.Van Aalten. Exploration of Starting Points For the Chemical Validation of Udp-N-Acetylglucosamine Pyrophosphorylase in Aspergillus Fumigatus To Be Published.