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Magnesium in PDB 4jp1: MG2+ Bound Structure of Vibrio Cholerae CHEY3

Protein crystallography data

The structure of MG2+ Bound Structure of Vibrio Cholerae CHEY3, PDB code: 4jp1 was solved by M.Biswas, J.Dasgupta, U.Sen, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 27.39 / 2.46
Space group H 3
Cell size a, b, c (Å), α, β, γ (°) 68.020, 68.020, 74.423, 90.00, 90.00, 120.00
R / Rfree (%) 23.5 / 24.3

Magnesium Binding Sites:

The binding sites of Magnesium atom in the MG2+ Bound Structure of Vibrio Cholerae CHEY3 (pdb code 4jp1). 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 MG2+ Bound Structure of Vibrio Cholerae CHEY3, PDB code: 4jp1:

Magnesium binding site 1 out of 1 in 4jp1

Go back to Magnesium Binding Sites List in 4jp1
Magnesium binding site 1 out of 1 in the MG2+ Bound Structure 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 MG2+ Bound Structure of Vibrio Cholerae CHEY3 within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg201

b:48.2
occ:1.00
O A:ASN62 2.0 80.6 1.0
OD1 A:ASP16 2.0 58.9 1.0
OD2 A:ASP60 2.2 61.6 1.0
CG A:ASP60 3.0 60.4 1.0
CG A:ASP16 3.0 60.7 1.0
C A:ASN62 3.1 80.6 1.0
OD1 A:ASP60 3.3 62.9 1.0
OD2 A:ASP16 3.3 63.0 1.0
OD2 A:ASP15 3.7 66.0 1.0
CB A:ASN62 3.8 68.5 1.0
CA A:ASN62 3.8 81.7 1.0
CB A:ASP60 4.1 60.9 1.0
O A:HOH372 4.1 68.9 1.0
N A:ASN62 4.2 81.7 1.0
N A:MET63 4.2 0.4 1.0
CG A:MET63 4.3 49.7 1.0
CG A:ASP15 4.3 65.9 1.0
N A:ASP16 4.3 49.1 1.0
CB A:ASP16 4.4 58.3 1.0
OD1 A:ASP15 4.4 67.9 1.0
O A:HOH342 4.5 68.9 1.0
CA A:MET63 4.6 0.7 1.0
CA A:ASP16 4.9 50.9 1.0

Reference:

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
Page generated: Mon Dec 14 19:00:38 2020

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