Magnesium in PDB 4hnq: Crystal Structure of the Mutant Q97A of Vibrio Cholerae CHEY3

The structure of Crystal Structure of the Mutant Q97A of Vibrio Cholerae CHEY3, PDB code: 4hnq was solved by M.Biswas, U.Sen, J.Dasgupta, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	23.07 / 2.40
Space group	H 3
Cell size a, b, c (Å), α, β, γ (°)	67.640, 67.640, 74.918, 90.00, 90.00, 120.00
R / Rfree (%)	22.5 / 25.2

The binding sites of Magnesium atom in the Crystal Structure of the Mutant Q97A of Vibrio Cholerae CHEY3 (pdb code 4hnq). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of the Mutant Q97A of Vibrio Cholerae CHEY3, PDB code: 4hnq:

Magnesium binding site 1 out of 1 in the Crystal Structure of the Mutant Q97A of Vibrio Cholerae CHEY3


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 Mutant Q97A of Vibrio Cholerae CHEY3 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg201 b:66.5 occ:1.00 OD2 A:ASP60 1.9 39.0 1.0 OD1 A:ASP16 2.1 46.0 1.0 O A:ASN62 2.5 39.8 1.0 O A:HOH332 3.0 43.3 1.0 CG A:ASP60 3.0 34.7 1.0 CG A:ASP16 3.2 44.4 1.0 OD1 A:ASP60 3.4 35.4 1.0 OD2 A:ASP16 3.6 47.6 1.0 C A:ASN62 3.7 41.6 1.0 ND2 A:ASN62 4.1 52.4 1.0 CB A:ASP60 4.2 34.5 1.0 CG A:MET63 4.3 33.3 1.0 OD2 A:ASP15 4.4 35.6 1.0 N A:ASP16 4.4 38.2 1.0 CB A:ASP16 4.5 42.0 1.0 CG A:ASN62 4.5 49.8 1.0 OD1 A:ASP15 4.5 37.0 1.0 N A:MET63 4.5 40.8 1.0 CA A:MET63 4.5 39.6 1.0 CG A:ASP15 4.6 35.5 1.0 N A:ASN62 4.6 41.9 1.0 CA A:ASN62 4.7 43.6 1.0 OD1 A:ASN62 4.7 53.8 1.0 CA A:ASP16 5.0 40.1 1.0 O A:HOH361 5.0 44.7 1.0

M.Biswas, S.Dey, S.Khamrui, U.Sen, J.Dasgupta. Conformational Barrier of CHEY3 and Inability of CHEY4 to Bind Flim Control the Flagellar Motor Action in Vibrio Cholerae. Plos One V. 8 73923 2013.
ISSN: ESSN 1932-6203
PubMed: 24066084
DOI: 10.1371/JOURNAL.PONE.0073923