Magnesium in PDB 1d1b: Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with O,P- Dinitrophenyl Aminopropyldiphosphate Beryllium Trifluoride.

The structure of Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with O,P- Dinitrophenyl Aminopropyldiphosphate Beryllium Trifluoride., PDB code: 1d1b was solved by A.M.Gulick, C.B.Bauer, J.B.Thoden, E.Pate, R.G.Yount, I.Rayment, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 2.00
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	103.880, 180.460, 54.070, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with O,P- Dinitrophenyl Aminopropyldiphosphate Beryllium Trifluoride. also contains other interesting chemical elements:

Fluorine

(F)

3 atoms

The binding sites of Magnesium atom in the Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with O,P- Dinitrophenyl Aminopropyldiphosphate Beryllium Trifluoride. (pdb code 1d1b). 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 Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with O,P- Dinitrophenyl Aminopropyldiphosphate Beryllium Trifluoride., PDB code: 1d1b:

Magnesium binding site 1 out of 1 in the Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with O,P- Dinitrophenyl Aminopropyldiphosphate Beryllium Trifluoride.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with O,P- Dinitrophenyl Aminopropyldiphosphate Beryllium Trifluoride. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg998 b:18.7 occ:1.00 OB2 A:DAQ999 2.0 11.8 1.0 OG1 A:THR186 2.0 25.4 1.0 OG A:SER237 2.0 21.7 1.0 O A:HOH1540 2.0 16.0 1.0 O A:HOH1541 2.1 13.8 1.0 F3 A:DAQ999 2.1 21.5 1.0 CB A:THR186 2.9 22.5 1.0 CB A:SER237 3.3 16.1 1.0 PB A:DAQ999 3.3 15.6 1.0 BE A:DAQ999 3.3 9.0 1.0 OB3 A:DAQ999 3.5 17.9 1.0 N A:SER237 3.8 15.8 1.0 N A:THR186 3.8 14.9 1.0 CA A:THR186 3.9 10.2 1.0 CG2 A:THR186 4.0 18.2 1.0 CA A:SER237 4.1 14.2 1.0 OA2 A:DAQ999 4.1 16.0 1.0 OD1 A:ASP454 4.1 20.2 1.0 F1 A:DAQ999 4.2 23.4 1.0 OA3 A:DAQ999 4.3 22.6 1.0 OB1 A:DAQ999 4.3 10.0 1.0 OD2 A:ASP454 4.4 20.4 1.0 F2 A:DAQ999 4.4 27.5 1.0 OA1 A:DAQ999 4.5 17.6 1.0 PA A:DAQ999 4.6 27.6 1.0 O A:HOH1056 4.6 19.2 1.0 O A:HOH1058 4.6 32.0 1.0 CB A:LYS185 4.6 13.2 1.0 CG A:ASP454 4.7 25.4 1.0 O A:ASN235 4.8 24.0 1.0 CE A:LYS185 4.8 19.8 1.0 ND2 A:ASN233 4.9 27.9 1.0 C A:SER236 4.9 13.6 1.0 C A:LYS185 4.9 17.3 1.0 O A:HOH1526 5.0 79.9 1.0

A.M.Gulick, C.B.Bauer, J.B.Thoden, E.Pate, R.G.Yount, I.Rayment. X-Ray Structures of the Dictyostelium Discoideum Myosin Motor Domain with Six Non-Nucleotide Analogs. J.Biol.Chem. V. 275 398 2000.
ISSN: ISSN 0021-9258
PubMed: 10617631
DOI: 10.1074/JBC.275.1.398