Magnesium 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:

Fluorine

(F)

12 atoms

The binding sites of Magnesium 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 Magnesium atom.
In total 4 binding sites of Magnesium 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 Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 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 Magnesium with other atoms in the Mg 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:Mg123 b:10.3 occ:1.00 O A:HOH148 2.0 10.6 1.0 F1 A:BFD53 2.0 7.3 0.8 OD1 A:ASP10 2.1 10.5 1.0 O A:HOH368 2.1 9.7 1.0 OD2 A:BFD53 2.1 8.9 1.0 O A:MET55 2.2 11.6 1.0 CG A:ASP10 3.1 12.8 1.0 CG A:BFD53 3.1 10.0 1.0 BE A:BFD53 3.2 7.3 0.8 C A:MET55 3.4 11.7 1.0 OD2 A:ASP10 3.5 15.5 1.0 OD1 A:BFD53 3.5 10.7 1.0 OD1 A:ASP9 4.0 10.5 1.0 CB A:MET55 4.1 12.3 1.0 CA A:MET55 4.1 12.6 1.0 O A:HOH493 4.1 30.6 1.0 F2 A:BFD53 4.1 5.7 0.8 O A:HOH409 4.1 21.4 1.0 O A:HOH376 4.1 20.7 1.0 CG A:MET56 4.2 11.9 1.0 N A:MET55 4.3 11.4 1.0 F3 A:BFD53 4.4 7.4 0.8 N A:MET56 4.4 11.8 1.0 N A:ASP10 4.4 11.0 1.0 CB A:ASP10 4.4 11.0 1.0 CB A:BFD53 4.5 8.8 1.0 NZ A:LYS105 4.5 11.9 1.0 CG A:ASP9 4.6 10.4 1.0 CA A:MET56 4.6 11.9 1.0 OD2 A:ASP9 4.7 10.0 1.0 CA A:ASP10 4.9 11.4 1.0

Magnesium binding site 2 out of 4 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 Magnesium with other atoms in the Mg 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 B:Mg123 b:8.8 occ:1.00 O B:HOH149 2.0 9.2 1.0 F1 B:BFD53 2.0 4.0 0.8 O B:MET55 2.0 8.8 1.0 OD2 B:BFD53 2.1 6.7 1.0 OD1 B:ASP10 2.1 9.2 1.0 O B:HOH369 2.2 9.0 1.0 CG B:BFD53 3.0 7.0 1.0 CG B:ASP10 3.2 10.8 1.0 BE B:BFD53 3.2 5.0 0.8 C B:MET55 3.2 8.3 1.0 OD1 B:BFD53 3.4 7.8 1.0 OD2 B:ASP10 3.6 13.4 1.0 CA B:MET55 3.9 8.6 1.0 CB B:MET55 4.0 8.5 1.0 OD1 B:ASP9 4.0 12.0 1.0 F2 B:BFD53 4.1 4.8 0.8 O B:HOH566 4.1 21.1 1.0 N B:MET55 4.2 7.8 1.0 CG B:MET56 4.2 9.5 1.0 N B:MET56 4.3 8.8 1.0 F3 B:BFD53 4.3 4.5 0.8 O B:HOH568 4.3 20.7 1.0 CB B:BFD53 4.4 6.4 1.0 N B:ASP10 4.4 8.7 1.0 O B:HOH517 4.5 38.5 1.0 CB B:ASP10 4.5 9.1 1.0 CA B:MET56 4.6 9.4 1.0 CG B:ASP9 4.6 9.1 1.0 NZ B:LYS105 4.6 8.3 1.0 OD2 B:ASP9 4.7 8.5 1.0 CA B:ASP10 4.9 9.6 1.0

Magnesium binding site 3 out of 4 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 Magnesium with other atoms in the Mg 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 C:Mg123 b:9.2 occ:1.00 F1 C:BFD53 2.0 5.5 0.8 OD2 C:BFD53 2.1 7.7 1.0 O C:HOH166 2.1 9.2 1.0 OD1 C:ASP10 2.1 8.0 1.0 O C:MET55 2.1 9.1 1.0 O C:HOH194 2.2 10.8 1.0 CG C:BFD53 3.0 7.1 1.0 CG C:ASP10 3.1 10.3 1.0 BE C:BFD53 3.1 5.7 0.8 C C:MET55 3.3 9.2 1.0 OD1 C:BFD53 3.3 6.8 1.0 OD2 C:ASP10 3.5 12.0 1.0 OD1 C:ASP9 4.0 8.1 1.0 CA C:MET55 4.0 9.7 1.0 F2 C:BFD53 4.0 4.4 0.8 CB C:MET55 4.1 9.0 1.0 O A:HOH545 4.1 20.8 1.0 CG C:MET56 4.2 8.3 1.0 N C:MET55 4.2 8.4 1.0 O C:HOH213 4.2 39.0 1.0 F3 C:BFD53 4.3 4.4 0.8 N C:MET56 4.4 9.4 1.0 N C:ASP10 4.4 8.7 1.0 CB C:BFD53 4.4 6.8 1.0 O D:HOH592 4.4 40.4 1.0 CB C:ASP10 4.5 9.5 1.0 CG C:ASP9 4.5 7.8 1.0 CA C:MET56 4.6 9.8 1.0 NZ C:LYS105 4.6 7.7 1.0 OD2 C:ASP9 4.6 7.3 1.0 CA C:ASP10 4.9 9.4 1.0 O A:HOH244 4.9 24.4 1.0 CB C:MET56 5.0 9.2 1.0

Magnesium binding site 4 out of 4 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 Magnesium with other atoms in the Mg 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 D:Mg123 b:12.4 occ:1.00 F1 D:BFD53 2.0 10.0 0.8 O D:MET55 2.1 12.3 1.0 OD2 D:BFD53 2.1 11.3 1.0 OD1 D:ASP10 2.1 18.2 1.0 O D:HOH174 2.1 15.6 1.0 O D:HOH157 2.2 12.6 1.0 CG D:BFD53 3.0 11.2 1.0 BE D:BFD53 3.1 10.0 0.8 CG D:ASP10 3.2 18.7 1.0 C D:MET55 3.2 12.3 1.0 OD1 D:BFD53 3.3 12.8 1.0 OD2 D:ASP10 3.6 19.6 1.0 CA D:MET55 3.9 13.4 1.0 CB D:MET55 4.0 12.5 1.0 OD1 D:ASP9 4.0 14.7 1.0 O D:HOH339 4.0 27.2 1.0 F2 D:BFD53 4.0 10.2 0.8 N D:MET55 4.1 11.6 1.0 F3 D:BFD53 4.2 9.3 0.8 CG D:MET56 4.2 12.1 1.0 N D:MET56 4.3 12.2 1.0 O D:HOH537 4.3 31.0 1.0 CB D:BFD53 4.4 9.7 1.0 N D:ASP10 4.5 16.7 1.0 CB D:ASP10 4.5 18.2 1.0 O D:HOH326 4.5 26.8 1.0 CA D:MET56 4.6 12.4 1.0 CG D:ASP9 4.6 14.6 1.0 NZ D:LYS105 4.6 20.3 1.0 OD2 D:ASP9 4.8 13.6 1.0 CA D:ASP10 5.0 18.4 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