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Magnesium in PDB 5oaw: Crystal Structure of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutase in Complex with Glcnac-6P and Magnesium

Enzymatic activity of Crystal Structure of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutase in Complex with Glcnac-6P and Magnesium

All present enzymatic activity of Crystal Structure of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutase in Complex with Glcnac-6P and Magnesium:
5.4.2.3;

Protein crystallography data

The structure of Crystal Structure of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutase in Complex with Glcnac-6P and Magnesium, PDB code: 5oaw was solved by O.G.Raimi, R.Hurtado-Guerrero, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 93.25 / 2.34
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 71.314, 84.815, 186.399, 90.00, 90.00, 90.00
R / Rfree (%) 21 / 27.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutase in Complex with Glcnac-6P and Magnesium (pdb code 5oaw). 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 Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutase in Complex with Glcnac-6P and Magnesium, PDB code: 5oaw:

Magnesium binding site 1 out of 1 in 5oaw

Go back to Magnesium Binding Sites List in 5oaw
Magnesium binding site 1 out of 1 in the Crystal Structure of Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutase in Complex with Glcnac-6P and Magnesium


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 Aspergillus Fumigatus N-Acetylphosphoglucosamine Mutase in Complex with Glcnac-6P and Magnesium within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg601

b:49.3
occ:1.00
 OD2 A:ASP288 2.0 44.4 1.0
O3P A:SEP69 2.0 86.9 1.0
OD1 A:ASP286 2.2 49.1 1.0
OD2 A:ASP284 2.2 42.4 1.0
OG A:SEP69 2.6 75.8 1.0
CG A:ASP288 2.9 43.3 1.0
P A:SEP69 2.9 92.5 1.0
CG A:ASP286 3.0 45.8 1.0
OD1 A:ASP288 3.1 43.4 1.0
OD2 A:ASP286 3.2 45.7 1.0
CG A:ASP284 3.3 39.5 1.0
CB A:SEP69 3.4 65.3 1.0
OD1 A:ASP284 3.7 39.4 1.0
O2P A:SEP69 3.8 87.9 1.0
O1P A:SEP69 4.1 84.2 1.0
CD A:ARG289 4.1 46.2 1.0
CA A:SEP69 4.2 63.1 1.0
CB A:ASP288 4.3 40.3 1.0
N A:ASP288 4.5 36.1 1.0
CB A:ASP286 4.5 38.0 1.0
CB A:ASP284 4.5 36.4 1.0
CG A:ARG289 4.5 45.0 1.0
CA A:ASP288 4.7 38.4 1.0
N A:ASP286 4.8 38.7 1.0
C A:ASP288 4.8 38.4 1.0
C A:SEP69 4.8 66.8 1.0
N A:ARG289 4.9 37.8 1.0
CA A:ASP286 5.0 39.2 1.0
N A:HIS70 5.0 65.2 1.0

Reference:

O.G.Raimi, R.Hurtado-Guerrero, D.M.F.Van Aalten. Evidence For Substrate-Assisted Catalysis Inn-Acetylphosphoglucosamine Mutase. Biochem. J. V. 475 2547 2018.
ISSN: ESSN 1470-8728
PubMed: 29967067
DOI: 10.1042/BCJ20180172
Page generated: Mon Sep 30 00:14:23 2024

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