Magnesium in PDB 1kk8: Scallop Myosin (S1-Adp-Befx) in the Actin-Detached Conformation

The structure of Scallop Myosin (S1-Adp-Befx) in the Actin-Detached Conformation, PDB code: 1kk8 was solved by M.Himmel, S.Gourinath, L.Reshetnikova, Y.Shen, G.Szent-Gyorgyi, C.Cohen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	29.84 / 2.30
Space group	P 1
Cell size a, b, c (Å), α, β, γ (°)	51.604, 58.527, 133.295, 81.08, 84.94, 67.24
R / Rfree (%)	23 / 26.9

The structure of Scallop Myosin (S1-Adp-Befx) in the Actin-Detached Conformation also contains other interesting chemical elements:

Fluorine	(F)	3 atoms
Calcium	(Ca)	1 atom

The binding sites of Magnesium atom in the Scallop Myosin (S1-Adp-Befx) in the Actin-Detached Conformation (pdb code 1kk8). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Scallop Myosin (S1-Adp-Befx) in the Actin-Detached Conformation, PDB code: 1kk8:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Scallop Myosin (S1-Adp-Befx) in the Actin-Detached Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Scallop Myosin (S1-Adp-Befx) in the Actin-Detached Conformation within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg997 b:29.4 occ:1.00 O A:HOH1042 2.0 24.4 1.0 F3 A:BEF995 2.0 39.1 1.0 OG A:SER241 2.1 37.6 1.0 O A:HOH1041 2.2 27.5 1.0 O2B A:ADP996 2.2 34.0 1.0 OG1 A:THR183 2.4 31.8 1.0 CB A:SER241 2.9 38.4 1.0 CB A:THR183 3.2 32.4 1.0 BE A:BEF995 3.3 35.7 1.0 PB A:ADP996 3.4 39.9 1.0 N A:SER241 3.4 38.0 1.0 O3B A:ADP996 3.5 37.6 1.0 CA A:SER241 3.7 39.4 1.0 O2A A:ADP996 4.0 34.7 1.0 OD2 A:ASP460 4.1 57.6 1.0 CG2 A:THR183 4.2 27.7 1.0 F2 A:BEF995 4.2 36.1 1.0 N A:THR183 4.3 30.8 1.0 O A:HOH1040 4.3 38.8 1.0 O3A A:ADP996 4.3 35.6 1.0 F1 A:BEF995 4.3 33.9 1.0 O A:HOH1083 4.3 49.1 1.0 CA A:THR183 4.4 31.2 1.0 O A:ASN239 4.4 33.0 1.0 O A:HOH1012 4.4 35.6 1.0 C A:SER240 4.5 36.9 1.0 O1B A:ADP996 4.5 35.0 1.0 ND2 A:ASN237 4.6 27.5 1.0 PA A:ADP996 4.6 32.4 1.0 O A:HOH1069 4.7 34.2 1.0 CA A:SER240 4.8 36.0 1.0 ND2 A:ASN231 4.9 34.5 1.0 O1A A:ADP996 4.9 32.5 1.0 C A:SER241 4.9 39.6 1.0

Magnesium binding site 2 out of 2 in the Scallop Myosin (S1-Adp-Befx) in the Actin-Detached Conformation


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Scallop Myosin (S1-Adp-Befx) in the Actin-Detached Conformation within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg998 b:61.3 occ:1.00 O B:PHE34 1.8 64.6 1.0 OD1 B:ASP32 2.0 79.7 1.0 OD1 B:ASP28 2.2 71.1 1.0 OD2 B:ASP39 2.4 87.9 1.0 OD1 B:ASP30 2.8 78.4 1.0 OD2 B:ASP30 3.0 77.6 1.0 CG B:ASP39 3.0 84.7 1.0 OD1 B:ASP39 3.0 88.0 1.0 C B:PHE34 3.0 62.7 1.0 CG B:ASP32 3.1 78.0 1.0 CG B:ASP30 3.2 77.4 1.0 CG B:ASP28 3.4 71.9 1.0 OD2 B:ASP32 3.7 80.1 1.0 N B:PHE34 3.9 62.4 1.0 CA B:PHE34 3.9 62.0 1.0 N B:VAL35 4.0 63.5 1.0 CA B:VAL35 4.1 63.1 1.0 OD2 B:ASP28 4.2 71.1 1.0 N B:SER36 4.2 63.4 1.0 CB B:ASP32 4.3 75.2 1.0 CB B:ASP39 4.3 78.7 1.0 CB B:ASP28 4.3 72.0 1.0 CB B:PHE34 4.4 59.6 1.0 OG B:SER36 4.5 63.8 1.0 CA B:ASP28 4.5 71.5 1.0 N B:ASP32 4.5 74.1 1.0 C B:VAL35 4.6 63.2 1.0 CB B:ASP30 4.6 76.5 1.0 N B:ASP30 4.8 75.8 1.0 CA B:ASP32 4.9 73.1 1.0 C B:ASP28 4.9 73.0 1.0 N B:GLY33 4.9 69.1 1.0 CB B:SER36 4.9 65.4 1.0 N B:ARG31 4.9 72.6 1.0

D.M.Himmel, S.Gourinath, L.Reshetnikova, Y.Shen, A.G.Szent-Gyorgyi, C.Cohen. Crystallographic Findings on the Internally Uncoupled and Near-Rigor States of Myosin: Further Insights Into the Mechanics of the Motor. Proc.Natl.Acad.Sci.Usa V. 99 12645 2002.
ISSN: ISSN 0027-8424
PubMed: 12297624
DOI: 10.1073/PNAS.202476799