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Magnesium in PDB 5g50: Vibrio Cholerae Scaffolding Protein Rbma in Complex with Magnesium.

Protein crystallography data

The structure of Vibrio Cholerae Scaffolding Protein Rbma in Complex with Magnesium., PDB code: 5g50 was solved by M.Maestre-Reyna, W.-J.Wu, C.-C.Lee, A.H.-J.Wang, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 46.56 / 2.30
Space group P 41 21 2
Cell size a, b, c (Å), α, β, γ (°) 123.513, 123.513, 100.526, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 23.7

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Vibrio Cholerae Scaffolding Protein Rbma in Complex with Magnesium. (pdb code 5g50). 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 Vibrio Cholerae Scaffolding Protein Rbma in Complex with Magnesium., PDB code: 5g50:

Magnesium binding site 1 out of 1 in 5g50

Go back to Magnesium Binding Sites List in 5g50
Magnesium binding site 1 out of 1 in the Vibrio Cholerae Scaffolding Protein Rbma in Complex with Magnesium.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Vibrio Cholerae Scaffolding Protein Rbma in Complex with Magnesium. within 5.0Å range:
probe atom residue distance (Å) B Occ
A:Mg1272

b:48.2
occ:1.00
O A:GLN50 2.3 37.3 1.0
OE1 A:GLN48 2.4 39.0 1.0
O A:HOH2010 2.6 41.3 1.0
O A:HOH2016 2.6 53.8 1.0
O A:HOH2015 2.6 42.3 1.0
O A:HOH2009 2.6 39.5 1.0
C A:GLN50 3.4 39.6 1.0
CD A:GLN48 3.5 37.1 1.0
O A:HOH2026 3.7 50.7 1.0
CB A:GLN50 4.1 48.7 1.0
CB A:GLN48 4.2 38.3 1.0
CA A:GLN50 4.2 42.9 1.0
CG A:GLN48 4.2 36.9 1.0
CG A:GLN50 4.2 55.1 1.0
N A:GLN50 4.3 41.3 1.0
NE2 A:GLN48 4.4 36.3 1.0
N A:LEU51 4.5 38.4 1.0
CA A:LEU51 4.7 37.5 1.0
CD2 A:LEU51 4.8 37.5 1.0
O A:HOH2017 4.8 51.8 1.0

Reference:

M.Maestre-Reyna, W.-J.Wu, C.-C.Lee, A.H.-J.Wang. Phosphate-Dependent Rbma Autoproteolysis Is Involved in Biofilm Dispersal of Vibrio Cholerae To Be Published.
Page generated: Mon Dec 14 20:20:27 2020

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