Magnesium in PDB 5t45: Chicken Smooth Muscle Myosin Motor Domain Co-Crystallized with the Specific Ck-571 Inhibitor, Mgadp.Befx Form

The structure of Chicken Smooth Muscle Myosin Motor Domain Co-Crystallized with the Specific Ck-571 Inhibitor, Mgadp.Befx Form, PDB code: 5t45 was solved by S.Sirigu, V.J.Planelles-Herrero, J.Hartman, A.Houdusse, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.35 / 2.80
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	72.940, 202.170, 67.020, 90.00, 90.00, 90.00
R / Rfree (%)	21.9 / 27.1

The structure of Chicken Smooth Muscle Myosin Motor Domain Co-Crystallized with the Specific Ck-571 Inhibitor, Mgadp.Befx Form also contains other interesting chemical elements:

Fluorine	(F)	4 atoms
Chlorine	(Cl)	1 atom

The binding sites of Magnesium atom in the Chicken Smooth Muscle Myosin Motor Domain Co-Crystallized with the Specific Ck-571 Inhibitor, Mgadp.Befx Form (pdb code 5t45). 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 Chicken Smooth Muscle Myosin Motor Domain Co-Crystallized with the Specific Ck-571 Inhibitor, Mgadp.Befx Form, PDB code: 5t45:

Magnesium binding site 1 out of 1 in the Chicken Smooth Muscle Myosin Motor Domain Co-Crystallized with the Specific Ck-571 Inhibitor, Mgadp.Befx Form


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Chicken Smooth Muscle Myosin Motor Domain Co-Crystallized with the Specific Ck-571 Inhibitor, Mgadp.Befx Form within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg902 b:38.1 occ:1.00 O1B A:ADP904 1.9 42.7 1.0 OG1 A:THR184 2.0 41.9 1.0 F2 A:BEF903 2.1 52.6 1.0 O A:HOH1004 2.2 23.6 1.0 OG A:SER246 2.3 51.9 1.0 O A:HOH1021 2.8 45.4 1.0 CB A:THR184 3.2 42.0 1.0 PB A:ADP904 3.3 46.2 1.0 CB A:SER246 3.3 43.0 1.0 BE A:BEF903 3.5 51.2 1.0 OD1 A:ASP465 3.5 61.4 1.0 N A:THR184 3.6 38.3 1.0 O2B A:ADP904 3.6 47.0 1.0 CA A:THR184 3.9 38.6 1.0 N A:SER246 4.1 42.8 1.0 O2A A:ADP904 4.2 46.9 1.0 OD2 A:ASP465 4.2 70.0 1.0 O3A A:ADP904 4.2 46.8 1.0 O3B A:ADP904 4.3 43.6 1.0 CG A:ASP465 4.3 61.8 1.0 CG2 A:THR184 4.3 39.9 1.0 CA A:SER246 4.3 41.2 1.0 CB A:LYS183 4.4 38.4 1.0 F3 A:BEF903 4.4 48.2 1.0 CE A:LYS183 4.4 44.8 1.0 F1 A:BEF903 4.5 52.6 1.0 O1A A:ADP904 4.6 54.6 1.0 O A:HOH1010 4.6 39.7 1.0 PA A:ADP904 4.6 47.7 1.0 NZ A:LYS183 4.6 47.8 1.0 C A:LYS183 4.6 42.7 1.0 O A:HOH1061 4.7 43.7 1.0 CA A:LYS183 5.0 38.5 1.0 O A:HOH1033 5.0 41.6 1.0

S.Sirigu, J.J.Hartman, V.J.Planelles-Herrero, V.Ropars, S.Clancy, X.Wang, G.Chuang, X.Qian, P.P.Lu, E.Barrett, K.Rudolph, C.Royer, B.P.Morgan, E.A.Stura, F.I.Malik, A.M.Houdusse. Highly Selective Inhibition of Myosin Motors Provides the Basis of Potential Therapeutic Application. Proc. Natl. Acad. Sci. V. 113 E7448 2016U.S.A..
ISSN: ESSN 1091-6490
PubMed: 27815532
DOI: 10.1073/PNAS.1609342113