Magnesium in PDB 3pn7: Visualizing New Hinges and A Potential Major Source of Compliance in the Lever Arm of Myosin

The structure of Visualizing New Hinges and A Potential Major Source of Compliance in the Lever Arm of Myosin, PDB code: 3pn7 was solved by J.H.Brown, V.S.Senthil-Kumar, E.O'neall-Hennessey, L.Reshetnikova, H.Robinson, M.Nguyen-Mccarty, A.G.Szent-Gyorgyi, C.Cohen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.67 / 2.25
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	50.737, 68.779, 79.305, 77.41, 85.94, 73.61
R / Rfree (%)	19.1 / 24.1

The structure of Visualizing New Hinges and A Potential Major Source of Compliance in the Lever Arm of Myosin also contains other interesting chemical elements:

Calcium

(Ca)

2 atoms

The binding sites of Magnesium atom in the Visualizing New Hinges and A Potential Major Source of Compliance in the Lever Arm of Myosin (pdb code 3pn7). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Visualizing New Hinges and A Potential Major Source of Compliance in the Lever Arm of Myosin, PDB code: 3pn7:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Visualizing New Hinges and A Potential Major Source of Compliance in the Lever Arm of Myosin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Visualizing New Hinges and A Potential Major Source of Compliance in the Lever Arm of Myosin within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg162 b:44.7 occ:1.00 OD2 B:ASP44 2.4 34.4 1.0 OD2 B:ASP33 2.4 34.8 1.0 O B:PHE39 2.5 37.0 1.0 CB B:ASN35 2.5 37.0 1.0 CB B:ASP37 2.5 39.5 1.0 OD1 B:ASN35 2.8 51.2 1.0 CG B:ASN35 3.0 47.4 1.0 OD2 B:ASP37 3.1 45.6 1.0 CG B:ASP37 3.3 43.5 1.0 CG B:ASP44 3.3 38.1 1.0 CG B:ASP33 3.6 34.5 1.0 C B:PHE39 3.6 29.6 1.0 OD1 B:ASP44 3.6 42.4 1.0 CA B:ASP37 3.8 39.8 1.0 CA B:ASN35 3.8 45.6 1.0 N B:ASP37 3.8 37.7 1.0 N B:ASN35 4.0 42.2 1.0 OD1 B:ASP33 4.1 32.2 1.0 N B:PHE39 4.2 36.1 1.0 ND2 B:ASN35 4.2 50.7 1.0 CA B:PHE39 4.3 33.1 1.0 C B:ASN35 4.4 40.8 1.0 OD1 B:ASP41 4.4 42.9 1.0 OD1 B:ASP37 4.5 57.9 1.0 N B:ILE40 4.5 31.3 1.0 N B:ASP41 4.5 35.2 1.0 CB B:PHE39 4.5 36.1 1.0 CA B:ILE40 4.5 28.9 1.0 N B:ARG36 4.6 37.4 1.0 CG B:ASP41 4.6 43.0 1.0 C B:ASP37 4.6 44.7 1.0 N B:GLY38 4.6 37.4 1.0 OD2 B:ASP41 4.6 50.4 1.0 CB B:ASP33 4.7 35.4 1.0 CB B:ASP44 4.7 33.5 1.0 CA B:ASP33 4.7 38.6 1.0 C B:ASP33 4.8 40.1 1.0 C B:ILE40 5.0 29.8 1.0

Magnesium binding site 2 out of 2 in the Visualizing New Hinges and A Potential Major Source of Compliance in the Lever Arm of Myosin


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Visualizing New Hinges and A Potential Major Source of Compliance in the Lever Arm of Myosin within 5.0Å range: probe atom residue distance (Å) B Occ E:Mg162 b:67.1 occ:1.00 O E:PHE39 2.4 67.3 1.0 OD2 E:ASP44 2.4 65.2 1.0 OD2 E:ASP37 2.6 61.9 1.0 OD1 E:ASN35 2.7 67.7 1.0 OD1 E:ASP33 2.8 56.2 1.0 OD2 E:ASP41 2.9 81.4 1.0 ND2 E:ASN35 3.0 67.8 1.0 C E:PHE39 3.2 65.5 1.0 CG E:ASN35 3.2 69.1 1.0 CG E:ASP37 3.3 63.2 1.0 CG E:ASP44 3.4 67.4 1.0 OD1 E:ASP37 3.4 68.7 1.0 CG E:ASP41 3.5 74.7 1.0 N E:ASP41 3.5 70.1 1.0 CB E:ASP41 3.6 72.4 1.0 CA E:ILE40 3.8 66.1 1.0 C E:ILE40 3.9 65.4 1.0 N E:ILE40 3.9 63.7 1.0 CG E:ASP33 4.0 59.6 1.0 OD1 E:ASP44 4.0 70.3 1.0 N E:PHE39 4.1 58.1 1.0 CA E:ASP41 4.1 70.7 1.0 CA E:PHE39 4.2 59.6 1.0 CB E:ASP44 4.3 65.8 1.0 OD1 E:ASP41 4.4 75.4 1.0 CB E:ASP37 4.6 63.0 1.0 CB E:PHE39 4.6 61.5 1.0 O E:ILE40 4.7 66.1 1.0 CB E:ASN35 4.7 62.7 1.0 OD2 E:ASP33 4.7 57.6 1.0 N E:ASP37 4.9 61.5 1.0 CB E:ASP33 4.9 59.3 1.0 CA E:ASP33 4.9 59.0 1.0 N E:GLY38 5.0 65.9 1.0

J.H.Brown, V.S.Senthil Kumar, E.O'neall-Hennessey, L.Reshetnikova, H.Robinson, M.Nguyen-Mccarty, A.G.Szent-Gyorgyi, C.Cohen. Visualizing Key Hinges and A Potential Major Source of Compliance in the Lever Arm of Myosin. Proc.Natl.Acad.Sci.Usa V. 108 114 2011.
ISSN: ISSN 0027-8424
PubMed: 21149681
DOI: 10.1073/PNAS.1016288107