Magnesium in PDB 6np1: Product State Mimicry Leads to Aminoglycoside Discrimination in An Antibiotic Acetyltransferase

All present enzymatic activity of Product State Mimicry Leads to Aminoglycoside Discrimination in An Antibiotic Acetyltransferase:
2.3.1.81;

The structure of Product State Mimicry Leads to Aminoglycoside Discrimination in An Antibiotic Acetyltransferase, PDB code: 6np1 was solved by P.Kumar, M.J.Cuneo, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	43.29 / 1.60
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	85.349, 86.576, 50.352, 90.00, 118.92, 90.00
R / Rfree (%)	20.7 / 23.8

The binding sites of Magnesium atom in the Product State Mimicry Leads to Aminoglycoside Discrimination in An Antibiotic Acetyltransferase (pdb code 6np1). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Product State Mimicry Leads to Aminoglycoside Discrimination in An Antibiotic Acetyltransferase, PDB code: 6np1:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Product State Mimicry Leads to Aminoglycoside Discrimination in An Antibiotic Acetyltransferase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Product State Mimicry Leads to Aminoglycoside Discrimination in An Antibiotic Acetyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:24.2 occ:0.53 O A:HOH514 1.8 28.0 1.0 O A:HOH460 2.4 24.3 1.0 OD2 A:ASP145 2.6 28.9 1.0 O A:HOH504 3.0 32.8 1.0 CG A:ASP145 3.4 26.8 1.0 OD1 A:ASP145 3.4 26.5 1.0 CE1 A:HIS171 4.3 26.8 1.0 NE2 A:HIS171 4.3 26.8 1.0 O A:THR71 4.3 27.2 1.0 O A:HOH533 4.5 25.1 1.0 O A:HOH589 4.5 40.5 1.0 ND2 A:ASN73 4.5 24.4 1.0 O A:HOH488 4.6 37.3 1.0 CB A:ASP145 4.8 24.9 1.0

Magnesium binding site 2 out of 2 in the Product State Mimicry Leads to Aminoglycoside Discrimination in An Antibiotic Acetyltransferase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Product State Mimicry Leads to Aminoglycoside Discrimination in An Antibiotic Acetyltransferase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg302 b:43.9 occ:1.00 O A:HOH605 2.0 44.3 1.0 O A:HOH574 2.1 40.8 1.0 O A:HOH465 2.1 33.1 1.0 O A:HOH580 2.1 44.5 1.0 O A:HOH581 2.3 42.0 1.0 O A:HOH521 2.6 47.0 1.0 O A:HOH526 4.1 51.7 1.0 O A:HOH466 4.1 38.4 1.0 O A:HOH439 4.2 40.6 1.0 O A:ARG124 4.3 28.5 1.0 O A:HOH506 4.4 37.2 1.0 O A:TYR126 4.4 31.7 1.0 O A:THR125 4.6 34.9 1.0 CA A:THR125 4.7 32.5 1.0 C A:THR125 4.8 33.1 1.0 O A:HOH433 5.0 37.0 1.0 O A:CYS129 5.0 33.4 1.0

P.Kumar, P.K.Agarwal, M.B.Waddell, T.Mittag, E.H.Serpersu, M.J.Cuneo. Low-Barrier and Canonical Hydrogen Bonds Modulate Activity and Specificity of A Catalytic Triad. Angew.Chem.Int.Ed.Engl. V. 58 16260 2019.
ISSN: ESSN 1521-3773
PubMed: 31515870
DOI: 10.1002/ANIE.201908535