Fluorine in PDB 1d0x: Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with M- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride.

The structure of Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with M- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride., PDB code: 1d0x 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 (°)	104.000, 180.500, 54.000, 90.00, 90.00, 90.00
R / Rfree (%)	n/a / n/a

The structure of Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with M- 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 M- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride. (pdb code 1d0x). 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 M- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride., PDB code: 1d0x:
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 M- 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 M- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride. within 5.0Å range: probe atom residue distance (Å) B Occ A:F999 b:20.2 occ:1.00 F1 A:MNQ999 0.0 20.2 1.0 BE A:MNQ999 1.5 32.4 1.0 F2 A:MNQ999 2.5 18.8 1.0 O A:HOH1437 2.5 53.7 1.0 OB3 A:MNQ999 2.5 22.6 1.0 F3 A:MNQ999 2.6 20.2 1.0 NZ A:LYS185 2.8 12.5 1.0 CA A:SER181 3.1 9.3 1.0 CB A:SER181 3.5 16.1 1.0 CE A:LYS185 3.5 17.5 1.0 PB A:MNQ999 3.6 17.3 1.0 OG A:SER181 3.7 19.1 1.0 N A:SER181 3.8 13.1 1.0 OB1 A:MNQ999 3.9 12.3 1.0 O A:HOH1712 3.9 13.8 1.0 OB2 A:MNQ999 4.1 13.1 1.0 O A:HOH1371 4.1 47.3 1.0 MG A:MG998 4.1 20.1 1.0 N A:GLY182 4.2 22.1 1.0 C A:SER181 4.2 22.5 1.0 O A:GLU180 4.2 14.3 1.0 C A:GLU180 4.3 13.7 1.0 OG A:SER236 4.4 19.9 1.0 O A:HOH1110 4.6 35.5 1.0 O A:SER237 4.7 21.1 1.0 N A:SER237 4.8 23.1 1.0 ND2 A:ASN233 4.9 18.9 1.0 CD A:LYS185 5.0 9.8 1.0 O A:GLY179 5.0 15.3 1.0 OA3 A:MNQ999 5.0 14.5 1.0

Fluorine binding site 2 out of 3 in the Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with M- 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 M- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride. within 5.0Å range: probe atom residue distance (Å) B Occ A:F999 b:18.8 occ:1.00 F2 A:MNQ999 0.0 18.8 1.0 BE A:MNQ999 1.5 32.4 1.0 MG A:MG998 2.0 20.1 1.0 F1 A:MNQ999 2.5 20.2 1.0 OB3 A:MNQ999 2.5 22.6 1.0 F3 A:MNQ999 2.6 20.2 1.0 O A:HOH1712 2.8 13.8 1.0 N A:SER237 2.9 23.1 1.0 OB2 A:MNQ999 2.9 13.1 1.0 OG A:SER237 2.9 17.1 1.0 O A:HOH1048 3.0 14.8 1.0 CB A:SER237 3.1 17.0 1.0 PB A:MNQ999 3.3 17.3 1.0 CA A:SER237 3.6 12.9 1.0 O A:HOH1437 3.8 53.7 1.0 O A:SER237 3.9 21.1 1.0 ND2 A:ASN233 3.9 18.9 1.0 C A:SER236 3.9 19.3 1.0 OG A:SER236 4.0 19.9 1.0 CA A:SER236 4.1 15.9 1.0 OG1 A:THR186 4.2 19.7 1.0 C A:SER237 4.2 15.8 1.0 OB1 A:MNQ999 4.3 12.3 1.0 NZ A:LYS185 4.4 12.5 1.0 OA3 A:MNQ999 4.4 14.5 1.0 O A:HOH1371 4.5 47.3 1.0 CE A:LYS185 4.6 17.5 1.0 CB A:SER236 4.6 21.5 1.0 OA2 A:MNQ999 4.7 19.0 1.0 O A:ASN235 4.8 21.4 1.0 O A:HOH1426 4.9 49.0 1.0 OG A:SER181 4.9 19.1 1.0

Fluorine binding site 3 out of 3 in the Dictyostelium Myosin S1DC (Motor Domain Fragment) Complexed with M- 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 M- Nitrophenyl Aminoethyldiphosphate Beryllium Trifluoride. within 5.0Å range: probe atom residue distance (Å) B Occ A:F999 b:20.2 occ:1.00 F3 A:MNQ999 0.0 20.2 1.0 BE A:MNQ999 1.6 32.4 1.0 OG A:SER181 2.5 19.1 1.0 OG A:SER236 2.5 19.9 1.0 OB3 A:MNQ999 2.5 22.6 1.0 F2 A:MNQ999 2.6 18.8 1.0 F1 A:MNQ999 2.6 20.2 1.0 ND2 A:ASN233 3.0 18.9 1.0 CB A:SER236 3.0 21.5 1.0 CA A:SER236 3.2 15.9 1.0 O A:HOH1437 3.4 53.7 1.0 CB A:SER181 3.4 16.1 1.0 CA A:SER181 3.6 9.3 1.0 N A:SER237 3.6 23.1 1.0 CB A:ASN233 3.7 19.6 1.0 N A:GLY182 3.7 22.1 1.0 CG A:ASN233 3.8 24.1 1.0 C A:SER236 4.0 19.3 1.0 C A:SER181 4.1 22.5 1.0 PB A:MNQ999 4.1 17.3 1.0 O A:HOH1115 4.3 26.3 1.0 N A:SER236 4.4 18.4 1.0 MG A:MG998 4.4 20.1 1.0 O A:HOH1048 4.5 14.8 1.0 O A:SER237 4.6 21.1 1.0 OB2 A:MNQ999 4.6 13.1 1.0 OA3 A:MNQ999 4.7 14.5 1.0 NH2 A:ARG238 4.8 19.8 1.0 CA A:SER237 4.8 12.9 1.0 CA A:GLY182 4.9 8.7 1.0 N A:SER181 4.9 13.1 1.0 O A:ASN235 5.0 21.4 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