Fluorine in PDB 1d0z: Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with P- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride.

The structure of Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with P- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride., PDB code: 1d0z 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 (°)	103.987, 180.855, 54.101, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with P- Nitrophenyl 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 P- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride. (pdb code 1d0z). 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 P- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride., PDB code: 1d0z:
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 P- Nitrophenyl 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 P- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride. within 5.0Å range: probe atom residue distance (Å) B Occ A:F999 b:15.6 occ:1.00 F1 A:PNQ999 0.0 15.6 1.0 BE A:PNQ999 1.5 18.1 1.0 F2 A:PNQ999 2.5 15.8 1.0 F3 A:PNQ999 2.5 13.6 1.0 OB3 A:PNQ999 2.6 13.4 1.0 O A:HOH1371 2.8 40.6 1.0 NZ A:LYS185 2.9 9.5 1.0 CA A:SER181 3.1 7.4 1.0 CB A:SER181 3.5 16.3 1.0 CE A:LYS185 3.6 9.0 1.0 OG A:SER181 3.7 13.9 1.0 PB A:PNQ999 3.7 11.8 1.0 N A:SER181 3.8 12.2 1.0 O A:HOH1149 3.9 41.8 1.0 O A:HOH1454 3.9 6.4 1.0 OB1 A:PNQ999 4.0 9.3 1.0 OB2 A:PNQ999 4.1 9.6 1.0 N A:GLY182 4.1 17.2 1.0 MG A:MG998 4.1 10.3 1.0 C A:SER181 4.2 21.4 1.0 O A:GLU180 4.3 11.3 1.0 C A:GLU180 4.3 12.8 1.0 O A:HOH1118 4.4 21.1 1.0 O A:SER237 4.6 14.0 1.0 OG A:SER236 4.6 14.3 1.0 N A:SER237 4.8 12.9 1.0 O A:GLY179 4.9 7.0 1.0 ND2 A:ASN233 4.9 9.8 1.0 CB A:SER237 5.0 19.3 1.0

Fluorine binding site 2 out of 3 in the Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with P- Nitrophenyl 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 P- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride. within 5.0Å range: probe atom residue distance (Å) B Occ A:F999 b:15.8 occ:1.00 F2 A:PNQ999 0.0 15.8 1.0 BE A:PNQ999 1.5 18.1 1.0 OB3 A:PNQ999 2.5 13.4 1.0 F1 A:PNQ999 2.5 15.6 1.0 F3 A:PNQ999 2.6 13.6 1.0 OG A:SER181 2.6 13.9 1.0 OG A:SER236 2.8 14.3 1.0 ND2 A:ASN233 3.1 9.8 1.0 CB A:SER236 3.3 18.8 1.0 O A:HOH1371 3.4 40.6 1.0 CA A:SER236 3.4 12.0 1.0 CB A:SER181 3.5 16.3 1.0 CA A:SER181 3.6 7.4 1.0 N A:GLY182 3.7 17.2 1.0 N A:SER237 3.7 12.9 1.0 CB A:ASN233 3.8 4.0 1.0 CG A:ASN233 3.8 14.1 1.0 C A:SER181 4.0 21.4 1.0 C A:SER236 4.1 25.5 1.0 PB A:PNQ999 4.1 11.8 1.0 MG A:MG998 4.4 10.3 1.0 O A:HOH1037 4.4 20.9 1.0 OB2 A:PNQ999 4.5 9.6 1.0 N A:SER236 4.5 11.3 1.0 O A:HOH1453 4.6 9.1 1.0 O A:SER237 4.6 14.0 1.0 CA A:GLY182 4.8 4.1 1.0 NH2 A:ARG238 4.8 23.2 1.0 OA3 A:PNQ999 4.8 12.5 1.0 CA A:SER237 4.8 7.9 1.0 N A:SER181 4.9 12.2 1.0 OB1 A:PNQ999 5.0 9.3 1.0 O A:ASN235 5.0 14.5 1.0

Fluorine binding site 3 out of 3 in the Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with P- Nitrophenyl 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 P- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride. within 5.0Å range: probe atom residue distance (Å) B Occ A:F999 b:13.6 occ:1.00 F3 A:PNQ999 0.0 13.6 1.0 BE A:PNQ999 1.5 18.1 1.0 MG A:MG998 2.0 10.3 1.0 F1 A:PNQ999 2.5 15.6 1.0 OB3 A:PNQ999 2.5 13.4 1.0 F2 A:PNQ999 2.6 15.8 1.0 O A:HOH1454 2.6 6.4 1.0 OG A:SER237 2.7 12.1 1.0 OB2 A:PNQ999 2.8 9.6 1.0 N A:SER237 2.9 12.9 1.0 O A:HOH1453 3.0 9.1 1.0 CB A:SER237 3.1 19.3 1.0 PB A:PNQ999 3.3 11.8 1.0 CA A:SER237 3.6 7.9 1.0 O A:SER237 3.9 14.0 1.0 ND2 A:ASN233 4.0 9.8 1.0 OG1 A:THR186 4.0 16.5 1.0 C A:SER236 4.0 25.5 1.0 O A:HOH1371 4.1 40.6 1.0 CA A:SER236 4.2 12.0 1.0 O A:HOH1149 4.2 41.8 1.0 OB1 A:PNQ999 4.3 9.3 1.0 C A:SER237 4.3 7.4 1.0 OG A:SER236 4.3 14.3 1.0 NZ A:LYS185 4.4 9.5 1.0 OA3 A:PNQ999 4.4 12.5 1.0 CE A:LYS185 4.6 9.0 1.0 OA2 A:PNQ999 4.7 8.9 1.0 O A:ASN235 4.8 14.5 1.0 CB A:SER236 4.8 18.8 1.0 CB A:THR186 5.0 11.1 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