Fluorine in PDB 1d1a: Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with O,P- Dinitrophenyl Aminoethyldiphosphate Beryllium Trifluoride.

The structure of Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with O,P- Dinitrophenyl Aminoethyldiphosphate Beryllium Trifluoride., PDB code: 1d1a 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 (°)	103.730, 180.001, 54.020, 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 Aminoethyldiphosphate Beryllium Trifluoride. also contains other interesting chemical elements:

Magnesium

(Mg)

1 atom

The binding sites of Fluorine atom in the Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with O,P- Dinitrophenyl Aminoethyldiphosphate Beryllium Trifluoride. (pdb code 1d1a). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 3 binding sites of Fluorine where determined in the Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with O,P- Dinitrophenyl Aminoethyldiphosphate Beryllium Trifluoride., PDB code: 1d1a:
Jump to Fluorine binding site number: 1; 2; 3;

Fluorine binding site 1 out of 3 in the Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with O,P- Dinitrophenyl Aminoethyldiphosphate Beryllium Trifluoride.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with O,P- Dinitrophenyl Aminoethyldiphosphate Beryllium Trifluoride. within 5.0Å range: probe atom residue distance (Å) B Occ A:F999 b:29.3 occ:1.00 F1 A:DAE999 0.0 29.3 1.0 BE A:DAE999 1.5 21.9 1.0 F2 A:DAE999 2.5 33.3 1.0 F3 A:DAE999 2.5 36.5 1.0 OB3 A:DAE999 2.5 21.0 1.0 NZ A:LYS185 2.8 20.5 1.0 CA A:SER181 3.0 28.3 1.0 CE A:LYS185 3.4 23.6 1.0 PB A:DAE999 3.6 22.8 1.0 CB A:SER181 3.6 14.5 1.0 OG A:SER181 3.6 21.5 1.0 O A:HOH1151 3.8 35.0 1.0 N A:SER181 3.8 23.4 1.0 OB2 A:DAE999 3.8 20.3 1.0 OB1 A:DAE999 3.8 19.1 1.0 O A:HOH996 3.9 16.9 1.0 N A:GLY182 3.9 29.9 1.0 C A:SER181 4.0 38.7 1.0 MG A:MG998 4.1 25.4 1.0 O A:HOH1347 4.2 74.8 1.0 O A:GLU180 4.2 25.5 1.0 C A:GLU180 4.3 17.5 1.0 OG A:SER236 4.5 24.1 1.0 O A:SER237 4.8 21.5 1.0 N A:SER237 4.8 32.6 1.0 ND2 A:ASN233 4.8 42.3 1.0 CD A:LYS185 4.9 20.1 1.0 O A:GLY179 4.9 23.1 1.0 OA3 A:DAE999 4.9 32.4 1.0 OG A:SER237 5.0 27.7 1.0

Fluorine binding site 2 out of 3 in the Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with O,P- Dinitrophenyl Aminoethyldiphosphate Beryllium Trifluoride.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with O,P- Dinitrophenyl Aminoethyldiphosphate Beryllium Trifluoride. within 5.0Å range: probe atom residue distance (Å) B Occ A:F999 b:33.3 occ:1.00 F2 A:DAE999 0.0 33.3 1.0 BE A:DAE999 1.5 21.9 1.0 MG A:MG998 2.0 25.4 1.0 F3 A:DAE999 2.5 36.5 1.0 F1 A:DAE999 2.5 29.3 1.0 OB3 A:DAE999 2.5 21.0 1.0 OB2 A:DAE999 2.7 20.3 1.0 OG A:SER237 2.8 27.7 1.0 N A:SER237 2.9 32.6 1.0 O A:HOH995 3.0 20.2 1.0 O A:HOH996 3.1 16.9 1.0 PB A:DAE999 3.3 22.8 1.0 CB A:SER237 3.4 15.4 1.0 CA A:SER237 3.6 26.5 1.0 C A:SER236 3.9 21.0 1.0 ND2 A:ASN233 3.9 42.3 1.0 CA A:SER236 4.0 35.2 1.0 OG1 A:THR186 4.0 34.1 1.0 O A:SER237 4.0 21.5 1.0 OG A:SER236 4.0 24.1 1.0 O A:HOH1151 4.2 35.0 1.0 OB1 A:DAE999 4.3 19.1 1.0 C A:SER237 4.4 16.8 1.0 OA3 A:DAE999 4.4 32.4 1.0 O A:ASN235 4.6 31.8 1.0 NZ A:LYS185 4.6 20.5 1.0 OA2 A:DAE999 4.6 22.7 1.0 CE A:LYS185 4.7 23.6 1.0 CB A:SER236 4.7 25.0 1.0 OG A:SER181 4.8 21.5 1.0 N A:GLY182 4.9 29.9 1.0 CG A:ASN233 5.0 36.4 1.0

Fluorine binding site 3 out of 3 in the Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with O,P- Dinitrophenyl Aminoethyldiphosphate Beryllium Trifluoride.


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with O,P- Dinitrophenyl Aminoethyldiphosphate Beryllium Trifluoride. within 5.0Å range: probe atom residue distance (Å) B Occ A:F999 b:36.5 occ:1.00 F3 A:DAE999 0.0 36.5 1.0 BE A:DAE999 1.5 21.9 1.0 F2 A:DAE999 2.5 33.3 1.0 OG A:SER181 2.5 21.5 1.0 OB3 A:DAE999 2.5 21.0 1.0 F1 A:DAE999 2.5 29.3 1.0 OG A:SER236 2.6 24.1 1.0 ND2 A:ASN233 3.0 42.3 1.0 CA A:SER236 3.4 35.2 1.0 CB A:SER236 3.4 25.0 1.0 CB A:SER181 3.4 14.5 1.0 CA A:SER181 3.5 28.3 1.0 N A:GLY182 3.5 29.9 1.0 N A:SER237 3.7 32.6 1.0 CG A:ASN233 3.8 36.4 1.0 CB A:ASN233 3.8 24.1 1.0 C A:SER181 3.9 38.7 1.0 C A:SER236 4.0 21.0 1.0 PB A:DAE999 4.1 22.8 1.0 O A:HOH1030 4.4 34.4 1.0 MG A:MG998 4.4 25.4 1.0 OB2 A:DAE999 4.4 20.3 1.0 N A:SER236 4.5 33.1 1.0 O A:HOH995 4.6 20.2 1.0 CA A:GLY182 4.6 19.3 1.0 O A:SER237 4.7 21.5 1.0 NH1 A:ARG238 4.8 35.0 1.0 N A:SER181 4.8 23.4 1.0 OD1 A:ASN233 4.8 36.3 1.0 OA3 A:DAE999 4.8 32.4 1.0 O A:ASN235 4.9 31.8 1.0 CA A:SER237 4.9 26.5 1.0 OB1 A:DAE999 5.0 19.1 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