Magnesium in PDB 1s5g: Structure of Scallop Myosin S1 Reveals A Novel Nucleotide Conformation

The structure of Structure of Scallop Myosin S1 Reveals A Novel Nucleotide Conformation, PDB code: 1s5g was solved by D.Risal, S.Gourinath, D.M.Himmel, 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)	43.44 / 3.10
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	84.051, 50.935, 161.590, 90.00, 98.36, 90.00
R / Rfree (%)	23.3 / 26.9

The structure of Structure of Scallop Myosin S1 Reveals A Novel Nucleotide Conformation also contains other interesting chemical elements:

Calcium

(Ca)

1 atom

The binding sites of Magnesium atom in the Structure of Scallop Myosin S1 Reveals A Novel Nucleotide Conformation (pdb code 1s5g). 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 Structure of Scallop Myosin S1 Reveals A Novel Nucleotide Conformation, PDB code: 1s5g:

Magnesium binding site 1 out of 1 in the Structure of Scallop Myosin S1 Reveals A Novel Nucleotide Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Structure of Scallop Myosin S1 Reveals A Novel Nucleotide Conformation within 5.0Å range: probe atom residue distance (Å) B Occ Y:Mg999 b:0.3 occ:1.00 OD2 Y:ASP39 2.6 0.7 1.0 OD2 Y:ASP30 2.7 0.7 1.0 OD1 Y:ASP32 2.8 0.7 1.0 CG Y:ASP32 2.9 0.9 1.0 OD2 Y:ASP32 3.0 0.1 1.0 OD1 Y:ASP30 3.2 0.6 1.0 CG Y:ASP30 3.3 0.9 1.0 CG Y:ASP39 3.7 0.0 1.0 CB Y:ASP32 3.9 0.5 1.0 N Y:SER36 4.4 0.4 1.0 O Y:PHE34 4.4 0.4 1.0 OD1 Y:ASP39 4.5 0.6 1.0 CB Y:SER36 4.6 0.3 1.0 CB Y:ASP39 4.7 0.4 1.0 CB Y:ASP30 4.8 0.2 1.0 CA Y:VAL35 4.9 0.3 1.0

D.Risal, S.Gourinath, D.M.Himmel, A.G.Szent-Gyorgyi, C.Cohen. Myosin Subfragment 1 Structures Reveal A Partially Bound Nucleotide and A Complex Salt Bridge That Helps Couple Nucleotide and Actin Binding. Proc.Natl.Acad.Sci.Usa V. 101 8930 2004.
ISSN: ISSN 0027-8424
PubMed: 15184651
DOI: 10.1073/PNAS.0403002101