Magnesium in PDB 6azr: Crystal Structure of the T264A HK853CP-BEF3-RR468 Complex

The structure of Crystal Structure of the T264A HK853CP-BEF3-RR468 Complex, PDB code: 6azr was solved by J.Rose, P.Zhou, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	45.50 / 3.63
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	178.458, 98.336, 71.458, 90.00, 109.80, 90.00
R / Rfree (%)	20.8 / 24

The structure of Crystal Structure of the T264A HK853CP-BEF3-RR468 Complex also contains other interesting chemical elements:

Fluorine

(F)

6 atoms

The binding sites of Magnesium atom in the Crystal Structure of the T264A HK853CP-BEF3-RR468 Complex (pdb code 6azr). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of the T264A HK853CP-BEF3-RR468 Complex, PDB code: 6azr:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the T264A HK853CP-BEF3-RR468 Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the T264A HK853CP-BEF3-RR468 Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg201 b:82.4 occ:1.00 F1 B:BFD53 2.1 0.5 1.0 OD1 B:ASP10 2.1 95.3 1.0 O B:MET55 2.3 93.5 1.0 OD2 B:BFD53 2.3 77.1 1.0 OD2 B:ASP10 2.4 85.2 1.0 CG B:ASP10 2.6 90.0 1.0 CG B:BFD53 3.3 83.2 1.0 BE B:BFD53 3.4 98.0 1.0 C B:MET55 3.5 94.2 1.0 OD1 B:BFD53 3.9 96.9 1.0 CB B:ASP10 4.1 85.9 1.0 F3 B:BFD53 4.1 99.4 1.0 OD1 B:ASP9 4.1 80.1 1.0 F2 B:BFD53 4.2 99.8 1.0 CB B:MET55 4.3 98.5 1.0 CG B:MET56 4.3 85.4 1.0 CA B:MET55 4.4 95.6 1.0 N B:MET56 4.4 95.8 1.0 N B:ASP10 4.5 81.5 1.0 CB B:BFD53 4.5 78.2 1.0 CA B:MET56 4.6 94.9 1.0 N B:MET55 4.6 93.9 1.0 CG B:ASP9 4.8 79.2 1.0 OD2 B:ASP9 4.8 79.0 1.0 CA B:ASP10 4.8 86.0 1.0 N B:SER11 4.9 80.0 1.0 NZ B:LYS105 5.0 72.1 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the T264A HK853CP-BEF3-RR468 Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the T264A HK853CP-BEF3-RR468 Complex within 5.0Å range: probe atom residue distance (Å) B Occ D:Mg201 b:76.8 occ:1.00 F1 D:BFD53 2.1 0.3 1.0 O D:MET55 2.3 92.8 1.0 OD2 D:BFD53 2.4 78.3 1.0 OD1 D:ASP10 2.4 97.0 1.0 OD2 D:ASP10 2.7 94.3 1.0 CG D:ASP10 2.9 94.7 1.0 BE D:BFD53 3.4 93.1 1.0 CG D:BFD53 3.5 80.6 1.0 C D:MET55 3.5 93.6 1.0 OD1 D:BFD53 3.9 93.3 1.0 F2 D:BFD53 3.9 91.5 1.0 CB D:MET55 3.9 94.5 1.0 OD2 D:ASP9 4.1 84.5 1.0 CA D:MET55 4.2 91.8 1.0 F3 D:BFD53 4.3 94.7 1.0 CB D:ASP10 4.4 87.7 1.0 N D:MET56 4.5 96.7 1.0 CG D:MET56 4.5 88.4 1.0 N D:MET55 4.5 87.3 1.0 NZ D:LYS105 4.6 66.3 1.0 OD1 D:ASP9 4.6 89.2 1.0 CG D:ASP9 4.6 89.1 1.0 N D:ASP10 4.7 84.0 1.0 CB D:BFD53 4.8 78.3 1.0 CA D:MET56 4.8 94.7 1.0

Y.Liu, J.Rose, S.Huang, Y.Hu, Q.Wu, D.Wang, C.Li, M.Liu, P.Zhou, L.Jiang. A pH-Gated Conformational Switch Regulates the Phosphatase Activity of Bifunctional Hiska-Family Histidine Kinases. Nat Commun V. 8 2104 2017.
ISSN: ESSN 2041-1723
PubMed: 29235472
DOI: 10.1038/S41467-017-02310-9