Magnesium in PDB 4bju: Genetic and Structural Validation of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutase As An Antifungal Target

All present enzymatic activity of Genetic and Structural Validation of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutase As An Antifungal Target:
5.4.2.3;

The structure of Genetic and Structural Validation of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutase As An Antifungal Target, PDB code: 4bju was solved by W.Fang, O.G.Raimi, R.Hurtado Guerrero, D.M.F.Van Aalten, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.69 / 2.35
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	74.700, 86.570, 185.420, 90.00, 90.00, 90.00
R / Rfree (%)	21.849 / 27.691

The binding sites of Magnesium atom in the Genetic and Structural Validation of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutase As An Antifungal Target (pdb code 4bju). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Genetic and Structural Validation of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutase As An Antifungal Target, PDB code: 4bju:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Genetic and Structural Validation of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutase As An Antifungal Target


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Genetic and Structural Validation of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutase As An Antifungal Target within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg998 b:5.3 occ:1.00 OD1 A:ASP288 1.9 19.1 1.0 OD2 A:ASP284 1.9 16.5 1.0 O2P A:SEP69 1.9 25.5 1.0 OD1 A:ASP286 1.9 15.6 1.0 OG A:SEP69 2.2 26.3 1.0 P A:SEP69 2.7 29.0 1.0 CG A:ASP288 2.8 19.5 1.0 CG A:ASP286 2.9 16.6 1.0 CG A:ASP284 3.1 16.7 1.0 OD2 A:ASP288 3.1 19.1 1.0 OD2 A:ASP286 3.2 16.9 1.0 CB A:SEP69 3.3 25.4 1.0 OD1 A:ASP284 3.6 16.7 1.0 O1P A:SEP69 3.7 28.1 1.0 O3P A:SEP69 3.8 28.1 1.0 CA A:SEP69 4.0 24.6 1.0 CD A:ARG289 4.1 24.9 1.0 CB A:ASP288 4.1 19.8 1.0 N A:ASP288 4.2 19.9 1.0 CB A:ASP284 4.3 16.7 1.0 CB A:ASP286 4.4 16.7 1.0 CG A:ARG289 4.4 24.4 1.0 CA A:ASP288 4.6 19.8 1.0 N A:ASP286 4.6 17.4 1.0 C A:SEP69 4.7 25.8 1.0 N A:ARG289 4.7 21.1 1.0 C A:ASP288 4.8 20.7 1.0 N A:HIS70 4.8 26.1 1.0 CA A:ASP286 4.8 17.6 1.0 C A:ASP286 4.9 19.0 1.0 N A:ALA287 4.9 19.3 1.0 CB A:ARG289 5.0 22.9 1.0

Magnesium binding site 2 out of 2 in the Genetic and Structural Validation of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutase As An Antifungal Target


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Genetic and Structural Validation of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutase As An Antifungal Target within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg998 b:5.1 occ:1.00 OD2 B:ASP284 1.8 17.2 1.0 O2P B:SEP69 1.9 24.3 1.0 OD1 B:ASP286 1.9 19.1 1.0 OD1 B:ASP288 2.0 22.8 1.0 OG B:SEP69 2.1 24.9 1.0 P B:SEP69 2.6 26.4 1.0 CG B:ASP284 3.0 17.7 1.0 CG B:ASP286 3.0 20.2 1.0 CG B:ASP288 3.0 21.7 1.0 OD2 B:ASP286 3.3 22.2 1.0 OD2 B:ASP288 3.3 21.4 1.0 CB B:SEP69 3.4 23.5 1.0 OD1 B:ASP284 3.6 17.2 1.0 O1P B:SEP69 3.7 25.9 1.0 O3P B:SEP69 3.7 25.1 1.0 CA B:SEP69 4.0 23.3 1.0 CD B:ARG289 4.1 28.2 1.0 CB B:ASP284 4.2 16.9 1.0 CB B:ASP288 4.3 21.0 1.0 CG B:ARG289 4.3 26.8 1.0 CB B:ASP286 4.4 19.3 1.0 N B:ASP288 4.4 20.1 1.0 N B:ASP286 4.6 18.9 1.0 C B:SEP69 4.6 23.4 1.0 CA B:ASP288 4.7 21.1 1.0 N B:HIS70 4.7 23.1 1.0 N B:ARG289 4.7 21.8 1.0 CA B:ASP286 4.8 19.5 1.0 C B:ASP288 4.8 22.4 1.0 CB B:ARG289 4.8 23.4 1.0 C B:ASP286 5.0 20.2 1.0

W.Fang, T.Du, O.G.Raimi, R.Hurtado Guerrero, K.Marino, A.F.M.Ibrahim, O.Albarbarawi, M.A.J.Ferguson, C.Jin, D.M.F.Van Aalten. Genetic and Structural Validation of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutase As An Antifungal Target. Biosci.Rep V. 33 63 2013.
ISSN: ISSN 0144-8463
PubMed: 23844980
DOI: 10.1042/BSR20130053