Fluorine in PDB 3gl9: The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism

The structure of The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism, PDB code: 3gl9 was solved by P.Casino, V.Rubio, A.Marina, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	25.00 / 1.80
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	155.233, 155.233, 34.482, 90.00, 90.00, 120.00
R / Rfree (%)	18.5 / 23.7

The structure of The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism also contains other interesting chemical elements:

Magnesium

(Mg)

4 atoms

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 12;

Binding sites:

The binding sites of Fluorine atom in the The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism (pdb code 3gl9). This binding sites where shown within 5.0 Angstroms radius around Fluorine atom.
In total 12 binding sites of Fluorine where determined in the The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism, PDB code: 3gl9:
Jump to Fluorine binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Fluorine binding site 1 out of 12 in the The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 1 of The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism within 5.0Å range: probe atom residue distance (Å) B Occ A:F53 b:7.3 occ:0.80 F1 A:BFD53 0.0 7.3 0.8 BE A:BFD53 1.5 7.3 0.8 MG A:MG123 2.0 10.3 1.0 F2 A:BFD53 2.5 5.7 0.8 F3 A:BFD53 2.6 7.4 0.8 OD1 A:BFD53 2.7 10.7 1.0 OD2 A:BFD53 2.8 8.9 1.0 O A:HOH148 3.0 10.6 1.0 O A:MET55 3.0 11.6 1.0 O A:HOH368 3.0 9.7 1.0 CG A:BFD53 3.1 10.0 1.0 O A:HOH409 3.2 21.4 1.0 CB A:MET55 3.3 12.3 1.0 N A:MET55 3.5 11.4 1.0 CA A:MET55 3.7 12.6 1.0 C A:MET55 3.7 11.7 1.0 O A:HOH617 3.9 44.2 1.0 CG A:MET55 4.0 14.2 1.0 CE A:MET55 4.0 16.7 1.0 OD1 A:ASP10 4.1 10.5 1.0 NZ A:LYS105 4.1 11.9 1.0 O A:HOH376 4.6 20.7 1.0 CB A:BFD53 4.6 8.8 1.0 C A:ILE54 4.6 10.9 1.0 N A:ILE54 4.6 9.7 1.0 SD A:MET55 4.8 15.7 1.0 OG1 A:THR83 5.0 11.3 1.0

Fluorine binding site 2 out of 12 in the The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 2 of The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism within 5.0Å range: probe atom residue distance (Å) B Occ A:F53 b:5.7 occ:0.80 F2 A:BFD53 0.0 5.7 0.8 BE A:BFD53 1.5 7.3 0.8 F3 A:BFD53 2.5 7.4 0.8 F1 A:BFD53 2.5 7.3 0.8 OD1 A:BFD53 2.6 10.7 1.0 NZ A:LYS105 2.8 11.9 1.0 N A:ALA84 2.8 14.0 1.0 O A:HOH409 3.1 21.4 1.0 CE A:LYS105 3.3 11.7 1.0 CA A:THR83 3.4 11.9 1.0 CD A:LYS105 3.5 12.8 1.0 O A:HOH617 3.6 44.2 1.0 C A:THR83 3.6 12.9 1.0 CG A:BFD53 3.7 10.0 1.0 OG1 A:THR83 3.7 11.3 1.0 CB A:ALA84 3.7 15.2 1.0 CA A:ALA84 3.9 15.5 1.0 O A:HOH368 3.9 9.7 1.0 CB A:THR83 4.0 12.0 1.0 OD2 A:BFD53 4.1 8.9 1.0 MG A:MG123 4.1 10.3 1.0 O A:LEU82 4.3 9.8 1.0 CG A:LYS105 4.6 13.8 1.0 N A:THR83 4.6 11.4 1.0 CE A:MET55 4.6 16.7 1.0 O A:HOH364 4.8 14.7 1.0 O A:THR83 4.8 12.4 1.0 OD2 A:ASP9 4.8 10.0 1.0 N A:ILE54 4.9 9.7 1.0 C A:LEU82 4.9 10.9 1.0 N A:LYS85 4.9 17.7 1.0 CB A:BFD53 4.9 8.8 1.0 C A:ALA84 5.0 16.8 1.0 N A:MET55 5.0 11.4 1.0

Fluorine binding site 3 out of 12 in the The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 3 of The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism within 5.0Å range: probe atom residue distance (Å) B Occ A:F53 b:7.4 occ:0.80 F3 A:BFD53 0.0 7.4 0.8 BE A:BFD53 1.5 7.3 0.8 O A:HOH617 2.2 44.2 1.0 F2 A:BFD53 2.5 5.7 0.8 OG1 A:THR83 2.6 11.3 1.0 F1 A:BFD53 2.6 7.3 0.8 OD1 A:BFD53 2.6 10.7 1.0 N A:MET55 2.9 11.4 1.0 N A:ILE54 3.2 9.7 1.0 CB A:THR83 3.4 12.0 1.0 CB A:ILE54 3.4 10.7 1.0 CG A:MET55 3.5 14.2 1.0 CA A:ILE54 3.6 10.3 1.0 CG A:BFD53 3.6 10.0 1.0 C A:ILE54 3.7 10.9 1.0 CB A:MET55 3.7 12.3 1.0 CA A:THR83 3.8 11.9 1.0 CA A:MET55 3.9 12.6 1.0 N A:ALA84 3.9 14.0 1.0 OD2 A:BFD53 4.1 8.9 1.0 CE A:MET55 4.2 16.7 1.0 C A:BFD53 4.3 9.3 1.0 CG1 A:ILE54 4.3 10.5 1.0 C A:THR83 4.4 12.9 1.0 MG A:MG123 4.4 10.3 1.0 CG2 A:ILE54 4.5 10.1 1.0 O A:MET55 4.6 11.6 1.0 CA A:BFD53 4.6 8.8 1.0 SD A:MET55 4.7 15.7 1.0 C A:MET55 4.7 11.7 1.0 CB A:BFD53 4.7 8.8 1.0 O A:HOH409 4.7 21.4 1.0 N A:LYS85 4.8 17.7 1.0 CG2 A:THR83 4.8 11.1 1.0 O A:LEU82 4.8 9.8 1.0 CG A:LYS85 4.8 19.0 1.0 O A:ILE54 4.9 10.9 1.0 NZ A:LYS105 5.0 11.9 1.0 CA A:ALA84 5.0 15.5 1.0

Fluorine binding site 4 out of 12 in the The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 4 of The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism within 5.0Å range: probe atom residue distance (Å) B Occ B:F53 b:4.0 occ:0.80 F1 B:BFD53 0.0 4.0 0.8 BE B:BFD53 1.5 5.0 0.8 MG B:MG123 2.0 8.8 1.0 F2 B:BFD53 2.4 4.8 0.8 F3 B:BFD53 2.6 4.5 0.8 OD1 B:BFD53 2.7 7.8 1.0 OD2 B:BFD53 2.9 6.7 1.0 O B:HOH149 2.9 9.2 1.0 O B:HOH369 2.9 9.0 1.0 O B:MET55 3.0 8.8 1.0 CG B:BFD53 3.1 7.0 1.0 O B:HOH568 3.1 20.7 1.0 CB B:MET55 3.2 8.5 1.0 N B:MET55 3.5 7.8 1.0 CA B:MET55 3.6 8.6 1.0 C B:MET55 3.7 8.3 1.0 CE B:MET55 4.0 11.3 1.0 OD1 B:ASP10 4.1 9.2 1.0 CG B:MET55 4.1 9.3 1.0 NZ B:LYS105 4.2 8.3 1.0 O B:HOH566 4.3 21.1 1.0 CB B:BFD53 4.6 6.4 1.0 C B:ILE54 4.7 7.6 1.0 N B:ILE54 4.7 6.8 1.0 SD B:MET55 4.7 11.0 1.0 OG1 B:THR83 5.0 7.9 1.0 N B:ALA84 5.0 8.1 1.0

Fluorine binding site 5 out of 12 in the The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 5 of The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism within 5.0Å range: probe atom residue distance (Å) B Occ B:F53 b:4.8 occ:0.80 F2 B:BFD53 0.0 4.8 0.8 BE B:BFD53 1.5 5.0 0.8 F1 B:BFD53 2.4 4.0 0.8 F3 B:BFD53 2.5 4.5 0.8 OD1 B:BFD53 2.6 7.8 1.0 N B:ALA84 2.8 8.1 1.0 NZ B:LYS105 2.9 8.3 1.0 O B:HOH568 2.9 20.7 1.0 CE B:LYS105 3.4 8.5 1.0 CA B:THR83 3.5 7.1 1.0 CB B:ALA84 3.5 10.1 1.0 CD B:LYS105 3.5 9.4 1.0 C B:THR83 3.6 7.5 1.0 OG1 B:THR83 3.7 7.9 1.0 CG B:BFD53 3.7 7.0 1.0 CA B:ALA84 3.7 9.8 1.0 O B:HOH369 3.8 9.0 1.0 MG B:MG123 4.1 8.8 1.0 OD2 B:BFD53 4.1 6.7 1.0 CB B:THR83 4.2 6.8 1.0 O B:HOH373 4.4 14.0 1.0 O B:LEU82 4.5 6.4 1.0 CE B:MET55 4.5 11.3 1.0 N B:THR83 4.7 6.7 1.0 CG B:LYS105 4.7 8.8 1.0 OD2 B:ASP9 4.8 8.5 1.0 O B:THR83 4.8 6.8 1.0 O B:HOH566 4.8 21.1 1.0 C B:ALA84 4.8 10.7 1.0 N B:LYS85 4.9 11.4 1.0 N B:ILE54 5.0 6.8 1.0 N B:MET55 5.0 7.8 1.0 CB B:BFD53 5.0 6.4 1.0

Fluorine binding site 6 out of 12 in the The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 6 of The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism within 5.0Å range: probe atom residue distance (Å) B Occ B:F53 b:4.5 occ:0.80 F3 B:BFD53 0.0 4.5 0.8 BE B:BFD53 1.5 5.0 0.8 F2 B:BFD53 2.5 4.8 0.8 OD1 B:BFD53 2.5 7.8 1.0 OG1 B:THR83 2.6 7.9 1.0 F1 B:BFD53 2.6 4.0 0.8 N B:MET55 2.8 7.8 1.0 N B:ILE54 3.2 6.8 1.0 CB B:THR83 3.5 6.8 1.0 CB B:ILE54 3.5 7.1 0.5 CB B:ILE54 3.5 6.9 0.5 CG B:BFD53 3.5 7.0 1.0 CA B:ILE54 3.5 7.2 0.5 CA B:ILE54 3.6 7.0 0.5 C B:ILE54 3.7 7.6 1.0 CB B:MET55 3.7 8.5 1.0 CG B:MET55 3.7 9.3 1.0 CA B:MET55 3.8 8.6 1.0 CA B:THR83 3.8 7.1 1.0 N B:ALA84 3.8 8.1 1.0 CE B:MET55 4.0 11.3 1.0 OD2 B:BFD53 4.1 6.7 1.0 MG B:MG123 4.3 8.8 1.0 C B:BFD53 4.3 6.7 1.0 C B:THR83 4.3 7.5 1.0 CG B:LYS85 4.4 12.4 1.0 CG1 B:ILE54 4.4 7.2 0.5 CG1 B:ILE54 4.5 6.7 0.5 CG2 B:ILE54 4.5 7.3 0.5 O B:MET55 4.5 8.8 1.0 CG2 B:ILE54 4.5 7.0 0.5 CA B:BFD53 4.6 6.1 1.0 N B:LYS85 4.6 11.4 1.0 C B:MET55 4.6 8.3 1.0 CB B:BFD53 4.7 6.4 1.0 O B:HOH568 4.7 20.7 1.0 SD B:MET55 4.7 11.0 1.0 CA B:ALA84 4.8 9.8 1.0 O B:ILE54 4.9 7.5 1.0 CG2 B:THR83 4.9 7.2 1.0 CB B:ALA84 4.9 10.1 1.0 O B:LEU82 4.9 6.4 1.0

Fluorine binding site 7 out of 12 in the The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 7 of The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism within 5.0Å range: probe atom residue distance (Å) B Occ C:F53 b:5.5 occ:0.80 F1 C:BFD53 0.0 5.5 0.8 BE C:BFD53 1.5 5.7 0.8 MG C:MG123 2.0 9.2 1.0 F2 C:BFD53 2.5 4.4 0.8 F3 C:BFD53 2.6 4.4 0.8 OD1 C:BFD53 2.7 6.8 1.0 OD2 C:BFD53 2.9 7.7 1.0 O C:HOH166 2.9 9.2 1.0 O C:MET55 3.0 9.1 1.0 O C:HOH194 3.0 10.8 1.0 CG C:BFD53 3.1 7.1 1.0 CB C:MET55 3.2 9.0 1.0 N C:MET55 3.4 8.4 1.0 CA C:MET55 3.6 9.7 1.0 C C:MET55 3.7 9.2 1.0 CE C:MET55 3.8 13.9 1.0 CG C:MET55 4.1 10.5 1.0 OD1 C:ASP10 4.1 8.0 1.0 NZ C:LYS105 4.1 7.7 1.0 O A:HOH545 4.3 20.8 1.0 O D:HOH592 4.4 40.4 1.0 C C:ILE54 4.6 8.2 1.0 CB C:BFD53 4.7 6.8 1.0 N C:ILE54 4.7 7.5 1.0 SD C:MET55 4.7 13.2 1.0 OG1 C:THR83 4.9 8.6 1.0

Fluorine binding site 8 out of 12 in the The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 8 of The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism within 5.0Å range: probe atom residue distance (Å) B Occ C:F53 b:4.4 occ:0.80 F2 C:BFD53 0.0 4.4 0.8 BE C:BFD53 1.5 5.7 0.8 F1 C:BFD53 2.5 5.5 0.8 F3 C:BFD53 2.5 4.4 0.8 OD1 C:BFD53 2.5 6.8 1.0 NZ C:LYS105 2.7 7.7 1.0 N C:ALA84 2.8 10.4 1.0 CA C:THR83 3.5 8.6 1.0 CE C:LYS105 3.5 6.5 1.0 OG1 C:THR83 3.6 8.6 1.0 C C:THR83 3.6 9.3 1.0 CB C:ALA84 3.6 11.6 1.0 CG C:BFD53 3.7 7.1 1.0 O C:HOH194 3.8 10.8 1.0 CA C:ALA84 3.8 12.3 1.0 CD C:LYS105 3.9 8.3 1.0 CB C:THR83 4.0 8.7 1.0 MG C:MG123 4.0 9.2 1.0 OD2 C:BFD53 4.1 7.7 1.0 CE C:MET55 4.4 13.9 1.0 O C:LEU82 4.4 6.2 1.0 O A:HOH363 4.6 12.3 1.0 N C:THR83 4.6 7.6 1.0 N C:LYS85 4.7 14.8 1.0 O A:HOH545 4.7 20.8 1.0 OD2 C:ASP9 4.7 7.3 1.0 O C:THR83 4.8 9.6 1.0 C C:ALA84 4.8 13.7 1.0 N C:ILE54 4.9 7.5 1.0 N C:MET55 4.9 8.4 1.0 CG C:LYS105 4.9 8.8 1.0 CB C:BFD53 4.9 6.8 1.0 C C:LEU82 5.0 7.3 1.0

Fluorine binding site 9 out of 12 in the The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 9 of The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism within 5.0Å range: probe atom residue distance (Å) B Occ C:F53 b:4.4 occ:0.80 F3 C:BFD53 0.0 4.4 0.8 BE C:BFD53 1.5 5.7 0.8 F2 C:BFD53 2.5 4.4 0.8 OD1 C:BFD53 2.6 6.8 1.0 F1 C:BFD53 2.6 5.5 0.8 OG1 C:THR83 2.6 8.6 1.0 N C:MET55 2.8 8.4 1.0 N C:ILE54 3.1 7.5 1.0 CB C:ILE54 3.4 7.8 0.5 CB C:ILE54 3.4 7.7 0.5 CB C:THR83 3.4 8.7 1.0 CA C:ILE54 3.5 7.8 0.5 CA C:ILE54 3.5 7.7 0.5 CG C:BFD53 3.6 7.1 1.0 C C:ILE54 3.6 8.2 1.0 CG C:MET55 3.7 10.5 1.0 CB C:MET55 3.7 9.0 1.0 CA C:MET55 3.8 9.7 1.0 CE C:MET55 3.9 13.9 1.0 CA C:THR83 3.9 8.6 1.0 N C:ALA84 4.0 10.4 1.0 OD2 C:BFD53 4.1 7.7 1.0 C C:BFD53 4.3 7.0 1.0 MG C:MG123 4.3 9.2 1.0 CG1 C:ILE54 4.3 7.7 0.5 CG C:LYS85 4.3 17.7 1.0 CG2 C:ILE54 4.4 7.5 0.5 CG2 C:ILE54 4.4 7.5 0.5 CG1 C:ILE54 4.4 7.4 0.5 C C:THR83 4.5 9.3 1.0 O C:MET55 4.5 9.1 1.0 CA C:BFD53 4.6 6.5 1.0 C C:MET55 4.6 9.2 1.0 SD C:MET55 4.6 13.2 1.0 CB C:BFD53 4.7 6.8 1.0 N C:LYS85 4.8 14.8 1.0 CD C:LYS85 4.8 17.8 1.0 O C:ILE54 4.8 8.5 1.0 CG2 C:THR83 4.8 7.2 1.0 O C:LEU82 4.9 6.2 1.0 NZ C:LYS105 4.9 7.7 1.0 CD1 C:ILE54 4.9 7.8 0.5

Fluorine binding site 10 out of 12 in the The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism


Mono view


Stereo pair view

A full contact list of Fluorine with other atoms in the F binding site number 10 of The Structure of A Histidine Kinase-Response Regulator Complex Sheds Light Into Two-Component Signaling and Reveals A Novel Cis Autophosphorylation Mechanism within 5.0Å range: probe atom residue distance (Å) B Occ D:F53 b:10.0 occ:0.80 F1 D:BFD53 0.0 10.0 0.8 BE D:BFD53 1.5 10.0 0.8 MG D:MG123 2.0 12.4 1.0 F2 D:BFD53 2.5 10.2 0.8 F3 D:BFD53 2.6 9.3 0.8 OD1 D:BFD53 2.8 12.8 1.0 O D:HOH157 2.9 12.6 1.0 O D:HOH174 3.0 15.6 1.0 O D:MET55 3.0 12.3 1.0 OD2 D:BFD53 3.0 11.3 1.0 O D:HOH339 3.1 27.2 1.0 CB D:MET55 3.2 12.5 1.0 CG D:BFD53 3.3 11.2 1.0 N D:MET55 3.5 11.6 1.0 CE D:MET55 3.6 18.6 1.0 CA D:MET55 3.6 13.4 1.0 C D:MET55 3.7 12.3 1.0 CG D:MET55 4.0 14.7 1.0 OD1 D:ASP10 4.1 18.2 1.0 NZ D:LYS105 4.2 20.3 1.0 O D:HOH326 4.3 26.8 1.0 SD D:MET55 4.6 17.9 1.0 C D:ILE54 4.6 11.7 1.0 O D:HOH537 4.6 31.0 1.0 N D:ILE54 4.7 10.7 1.0 CB D:BFD53 4.8 9.7 1.0 OG1 D:THR83 4.9 10.4 1.0

P.Casino, V.Rubio, A.Marina. Structural Insight Into Partner Specificity and Phosphoryl Transfer in Two-Component Signal Transduction Cell(Cambridge,Mass.) V. 139 325 2009.
ISSN: ISSN 0092-8674
PubMed: 19800110
DOI: 10.1016/J.CELL.2009.08.032