Magnesium in PDB 9h5p: Crystal Structure of Thermoanaerobacterales Bacterium Monoamine Oxidase in Complex with Putrescine

The structure of Crystal Structure of Thermoanaerobacterales Bacterium Monoamine Oxidase in Complex with Putrescine, PDB code: 9h5p was solved by L.Basile, C.Poli, L.L.Santema, R.C.Lesenciuc, M.W.Fraaije, C.Binda, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	60.40 / 2.30
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	68.816, 100.338, 120.845, 90, 90, 90
R / Rfree (%)	20.3 / 27.5

The binding sites of Magnesium atom in the Crystal Structure of Thermoanaerobacterales Bacterium Monoamine Oxidase in Complex with Putrescine (pdb code 9h5p). 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 Thermoanaerobacterales Bacterium Monoamine Oxidase in Complex with Putrescine, PDB code: 9h5p:

Magnesium binding site 1 out of 1 in the Crystal Structure of Thermoanaerobacterales Bacterium Monoamine Oxidase in Complex with Putrescine


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 Thermoanaerobacterales Bacterium Monoamine Oxidase in Complex with Putrescine within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:53.0 occ:1.00 O A:HOH622 2.1 31.8 1.0 O A:HOH636 2.1 33.6 1.0 O A:HOH603 2.5 40.9 1.0 O A:THR84 2.7 41.0 1.0 O A:HOH670 3.0 35.1 1.0 C A:THR84 3.5 36.2 1.0 CA A:THR84 3.6 38.3 1.0 CB A:THR84 4.2 36.5 1.0 CG2 A:THR84 4.3 34.7 1.0 OD1 A:ASP88 4.5 39.7 1.0 OD2 A:ASP88 4.5 42.1 1.0 OD1 A:ASP102 4.7 59.3 1.0 N A:GLU85 4.8 36.9 1.0 O A:PRO83 4.9 32.1 1.0 N A:THR84 4.9 33.7 1.0 CG A:ASP88 5.0 42.4 1.0

L.Basile, C.Poli, L.L.Santema, R.C.Lesenciuc, M.W.Fraaije, C.Binda. Altering Substrate Specificity of A Thermostable Bacterial Monoamine Oxidase By Structure-Based Mutagenesis. Arch.Biochem.Biophys. V. 764 10276 2024.
ISSN: ESSN 1096-0384
PubMed: 39706511
DOI: 10.1016/J.ABB.2024.110276