Magnesium in PDB 6n4t: Crystal Structure of MATRIPTASE1 in Complex with A Peptidomimetic Benzothiazole

All present enzymatic activity of Crystal Structure of MATRIPTASE1 in Complex with A Peptidomimetic Benzothiazole:
3.4.21.109;

The structure of Crystal Structure of MATRIPTASE1 in Complex with A Peptidomimetic Benzothiazole, PDB code: 6n4t was solved by N.Campobasso, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.58 / 1.95
Space group	C 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	67.029, 141.519, 52.109, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 22.5

The binding sites of Magnesium atom in the Crystal Structure of MATRIPTASE1 in Complex with A Peptidomimetic Benzothiazole (pdb code 6n4t). 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 MATRIPTASE1 in Complex with A Peptidomimetic Benzothiazole, PDB code: 6n4t:

Magnesium binding site 1 out of 1 in the Crystal Structure of MATRIPTASE1 in Complex with A Peptidomimetic Benzothiazole


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 MATRIPTASE1 in Complex with A Peptidomimetic Benzothiazole within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:50.1 occ:1.00 OE1 A:GLU24 2.4 41.4 1.0 CD A:GLU24 3.2 33.5 1.0 CE A:MET117 3.7 28.3 1.0 OE2 A:GLU24 3.8 37.9 1.0 SD A:MET117 3.9 46.6 1.0 O A:HOH460 3.9 25.0 1.0 O A:PRO78 4.0 16.5 1.0 CG A:GLU24 4.2 32.5 1.0 CG A:MET117 4.4 25.7 1.0 O A:HOH553 4.9 22.2 1.0 C A:PRO78 4.9 17.3 1.0

F.Beliveau, A.Tarkar, S.P.Dion, A.Desilets, M.G.Ghinet, P.L.Boudreault, C.St-Georges, E.Marsault, D.Paone, J.Collins, C.H.Macphee, N.Campobasso, A.Groy, J.Cottom, M.Ouellette, A.J.Pope, R.Leduc. Discovery and Development of TMPRSS6 Inhibitors Modulating Hepcidin Levels in Human Hepatocytes. Cell Chem Biol V. 26 1559 2019.
ISSN: ESSN 2451-9456
PubMed: 31543462
DOI: 10.1016/J.CHEMBIOL.2019.09.004