Mercury in PDB 2fxm: Structure of the Human Beta-Myosin S2 Fragment

The structure of Structure of the Human Beta-Myosin S2 Fragment, PDB code: 2fxm was solved by W.Blankenfeldt, N.H.Thoma, J.S.Wray, M.Gautel, I.Schlichting, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.70
Space group	C 2 2 21
Cell size a, b, c (Å), α, β, γ (°)	40.290, 45.970, 373.700, 90.00, 90.00, 90.00
R / Rfree (%)	24.2 / 28.3

The binding sites of Mercury atom in the Structure of the Human Beta-Myosin S2 Fragment (pdb code 2fxm). This binding sites where shown within 5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Structure of the Human Beta-Myosin S2 Fragment, PDB code: 2fxm:
Jump to Mercury binding site number: 1; 2;

Mercury binding site 1 out of 2 in the Structure of the Human Beta-Myosin S2 Fragment


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 1 of Structure of the Human Beta-Myosin S2 Fragment within 5.0Å range: probe atom residue distance (Å) B Occ A:Hg2 b:87.8 occ:0.30 SG B:CYS905 2.3 95.3 1.0 SG A:CYS905 2.3 96.9 1.0 O A:ALA901 3.2 52.2 1.0 CB B:CYS905 3.3 65.7 1.0 CA B:CYS905 3.3 42.6 1.0 N B:CYS905 3.4 56.6 1.0 CB A:CYS905 3.4 61.5 1.0 N A:CYS905 3.4 57.1 1.0 CA A:CYS905 3.5 54.1 1.0 O B:ALA901 3.5 49.2 1.0 C A:ARG904 4.1 59.8 1.0 C A:ALA901 4.2 54.7 1.0 C B:ARG904 4.3 41.5 1.0 CB A:ARG904 4.3 79.4 1.0 C B:ALA901 4.4 47.6 1.0 O A:ARG904 4.7 69.4 1.0 CB B:ARG904 4.7 73.4 1.0 CA A:ARG904 4.8 60.1 1.0 C B:CYS905 4.8 66.4 1.0 CD1 B:LEU908 4.8 50.5 1.0 CA A:ALA901 4.9 44.1 1.0 CD1 A:LEU908 4.9 43.5 1.0 NH1 A:ARG904 4.9 72.8 1.0 O B:ARG904 4.9 55.1 1.0

Mercury binding site 2 out of 2 in the Structure of the Human Beta-Myosin S2 Fragment


Mono view


Stereo pair view

A full contact list of Mercury with other atoms in the Hg binding site number 2 of Structure of the Human Beta-Myosin S2 Fragment within 5.0Å range: probe atom residue distance (Å) B Occ B:Hg1 b:98.0 occ:0.30 SG B:CYS947 2.3 0.2 1.0 SG A:CYS947 2.3 99.5 1.0 CB B:CYS947 3.2 70.9 1.0 CA B:CYS947 3.3 77.5 1.0 N B:CYS947 3.3 51.8 1.0 CB A:CYS947 3.5 81.8 1.0 O B:LEU943 3.5 66.7 1.0 N A:CYS947 3.5 81.4 1.0 CA A:CYS947 3.6 80.4 1.0 O A:LEU943 3.6 96.8 1.0 C B:GLU946 4.2 60.9 1.0 C A:GLU946 4.3 70.4 1.0 C B:LEU943 4.4 62.1 1.0 CB A:GLU946 4.5 82.4 1.0 CB B:GLU946 4.5 71.7 1.0 C A:LEU943 4.6 69.6 1.0 CD1 A:LEU950 4.8 81.3 1.0 O B:GLU946 4.8 70.0 1.0 C B:CYS947 4.8 69.0 1.0 O A:GLU946 4.8 95.3 1.0 CA B:GLU946 4.9 61.5 1.0 CD1 B:LEU950 4.9 67.5 1.0 OE1 A:GLU946 5.0 0.2 1.0 CA A:GLU946 5.0 69.9 1.0 CD2 A:LEU943 5.0 58.2 1.0

W.Blankenfeldt, N.H.Thoma, J.S.Wray, M.Gautel, I.Schlichting. Crystal Structures of Human Cardiac {Beta}-Myosin II S2-{Delta} Provide Insight Into the Functional Role of the S2 Subfragment Proc.Natl.Acad.Sci.Usa V. 103 17713 2006.
ISSN: ISSN 0027-8424
PubMed: 17095604
DOI: 10.1073/PNAS.0606741103