Calcium in PDB 3ts5: Crystal Structure of A Light Chain Domain of Scallop Smooth Muscle Myosin

The structure of Crystal Structure of A Light Chain Domain of Scallop Smooth Muscle Myosin, PDB code: 3ts5 was solved by V.S.S.Kumar, E.O'neall-Hennessey, L.Reshetnikova, J.H.Brown, H.Robinson, 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)	48.75 / 2.39
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	50.811, 68.775, 79.418, 77.33, 85.99, 73.65
R / Rfree (%)	19.1 / 24.1

The structure of Crystal Structure of A Light Chain Domain of Scallop Smooth Muscle Myosin also contains other interesting chemical elements:

Magnesium

(Mg)

2 atoms

The binding sites of Calcium atom in the Crystal Structure of A Light Chain Domain of Scallop Smooth Muscle Myosin (pdb code 3ts5). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of A Light Chain Domain of Scallop Smooth Muscle Myosin, PDB code: 3ts5:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of A Light Chain Domain of Scallop Smooth Muscle Myosin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of A Light Chain Domain of Scallop Smooth Muscle Myosin within 5.0Å range: probe atom residue distance (Å) B Occ C:Ca157 b:43.5 occ:1.00 OD1 C:ASP25 2.2 32.8 1.0 O C:ALA27 2.4 42.7 1.0 OD2 C:ASP22 2.4 40.5 1.0 O C:GLY23 2.4 42.6 1.0 OD1 C:ASP19 2.4 39.6 1.0 O C:HOH196 2.6 42.9 1.0 O C:ASP19 2.7 37.0 1.0 CG C:ASP25 3.3 38.0 1.0 C C:GLY23 3.4 41.6 1.0 C C:ASP19 3.5 39.8 1.0 CG C:ASP22 3.5 40.5 1.0 C C:ALA27 3.5 46.3 1.0 CA C:ASP19 3.5 34.3 1.0 CG C:ASP19 3.6 40.4 1.0 OD2 C:ASP25 3.7 44.4 1.0 N C:ASP25 3.8 41.9 1.0 N C:ALA27 4.0 44.7 1.0 C C:ASP22 4.0 38.3 1.0 N C:GLY23 4.0 41.4 1.0 O C:HOH183 4.1 47.6 1.0 CB C:ASP19 4.1 34.5 1.0 N C:ARG24 4.1 32.3 1.0 CA C:ARG24 4.2 33.5 1.0 OD1 C:ASP22 4.2 47.3 1.0 CA C:ALA27 4.2 47.9 1.0 O C:ASP22 4.3 42.9 1.0 CA C:GLY23 4.3 39.3 1.0 C C:ARG24 4.4 39.5 1.0 CB C:ASP22 4.5 38.4 1.0 CB C:ASP25 4.5 36.5 1.0 CA C:ASP22 4.6 38.5 1.0 N C:GLY26 4.6 37.8 1.0 N C:VAL28 4.6 42.3 1.0 OD2 C:ASP19 4.6 42.7 1.0 CB C:ALA27 4.6 48.0 1.0 CA C:ASP25 4.6 37.7 1.0 N C:ASP22 4.6 33.9 1.0 O C:PHE18 4.7 36.2 1.0 N C:PHE20 4.7 34.9 1.0 CA C:VAL28 4.8 39.9 1.0 N C:ASP19 4.8 35.2 1.0 C C:ASP25 4.9 36.7 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of A Light Chain Domain of Scallop Smooth Muscle Myosin


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of A Light Chain Domain of Scallop Smooth Muscle Myosin within 5.0Å range: probe atom residue distance (Å) B Occ F:Ca157 b:44.2 occ:1.00 OD1 F:ASP22 2.3 42.8 1.0 O F:ASP19 2.5 44.0 1.0 O F:ALA27 2.5 42.0 1.0 OD1 F:ASP25 2.5 48.0 1.0 OD1 F:ASP19 2.5 42.8 1.0 O F:GLY23 2.5 50.3 1.0 O F:HOH164 2.6 37.4 1.0 C F:ASP19 3.3 43.6 1.0 CA F:ASP19 3.4 38.4 1.0 CG F:ASP25 3.4 53.3 1.0 C F:GLY23 3.5 46.8 1.0 CG F:ASP22 3.6 43.8 1.0 CG F:ASP19 3.6 48.6 1.0 C F:ALA27 3.6 42.9 1.0 O F:ASP22 3.8 42.0 1.0 OD2 F:ASP25 3.8 45.6 1.0 C F:ASP22 3.8 44.4 1.0 N F:ASP25 3.9 49.1 1.0 N F:GLY23 4.0 41.2 1.0 CB F:ASP19 4.0 41.2 1.0 N F:ALA27 4.2 48.1 1.0 CA F:GLY23 4.2 39.2 1.0 OD2 F:ASP22 4.3 41.9 1.0 N F:ARG24 4.3 47.8 1.0 O F:ASP25 4.3 63.6 1.0 CA F:ALA27 4.4 47.8 1.0 CA F:ARG24 4.4 47.9 1.0 CA F:ASP22 4.5 44.1 1.0 C F:ARG24 4.5 52.3 1.0 CB F:ASP22 4.5 38.3 1.0 N F:PHE20 4.6 41.3 1.0 N F:ASP22 4.6 41.9 1.0 O F:PHE18 4.6 39.6 1.0 C F:ASP25 4.6 56.4 1.0 CB F:ASP25 4.6 56.0 1.0 N F:VAL28 4.6 44.8 1.0 N F:ASP19 4.7 39.5 1.0 CA F:ASP25 4.7 52.4 1.0 OD2 F:ASP19 4.7 51.8 1.0 CA F:VAL28 4.8 42.2 1.0 CB F:ALA27 5.0 45.6 1.0

V.S.Senthil Kumar, E.O'neall-Hennessey, L.Reshetnikova, J.H.Brown, H.Robinson, A.G.Szent-Gyorgyi, C.Cohen. Crystal Structure of A Phosphorylated Light Chain Domain of Scallop Smooth-Muscle Myosin. Biophys.J. V. 101 2185 2011.
ISSN: ISSN 0006-3495
PubMed: 22067157
DOI: 10.1016/J.BPJ.2011.09.028