Magnesium in PDB 4kg0: Crystal Structure of the Drosophila Melanogaster Neuralized-NHR1 Domain

The structure of Crystal Structure of the Drosophila Melanogaster Neuralized-NHR1 Domain, PDB code: 4kg0 was solved by D.Gupta, M.T.Ehebauer, D.Y.Chirgadze, V.M.Bolanos-Garcia, T.L.Blundell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	38.66 / 2.10
Space group	P 65
Cell size a, b, c (Å), α, β, γ (°)	89.280, 89.280, 36.930, 90.00, 90.00, 120.00
R / Rfree (%)	16.3 / 23.1

The binding sites of Magnesium atom in the Crystal Structure of the Drosophila Melanogaster Neuralized-NHR1 Domain (pdb code 4kg0). 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 Drosophila Melanogaster Neuralized-NHR1 Domain, PDB code: 4kg0:

Magnesium binding site 1 out of 1 in the Crystal Structure of the Drosophila Melanogaster Neuralized-NHR1 Domain


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 Drosophila Melanogaster Neuralized-NHR1 Domain within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg301 b:42.0 occ:1.00 O A:HOH480 1.9 40.0 1.0 O A:HOH479 2.0 38.8 1.0 O A:HOH478 2.1 48.1 1.0 OE2 A:GLU130 2.2 39.9 1.0 OD1 A:ASN116 2.2 37.6 1.0 O A:HOH488 2.4 40.4 1.0 CG A:ASN116 3.2 39.6 1.0 CD A:GLU130 3.3 45.9 1.0 ND2 A:ASN116 3.6 29.5 1.0 CG A:GLU130 3.8 43.2 1.0 O A:HOH505 4.0 57.6 1.0 OE1 A:GLU130 4.4 48.2 1.0 O A:ASP115 4.4 39.0 1.0 O A:HOH481 4.5 53.5 1.0 CB A:ASN116 4.6 33.9 1.0 CB A:ASP115 4.8 43.1 1.0 C A:ASP115 4.8 39.6 1.0 CA A:ASN116 4.8 34.8 1.0 O A:HOH490 4.9 67.9 1.0 N A:ASN116 5.0 34.9 1.0 CZ A:PHE129 5.0 40.8 1.0

D.Gupta, S.Beaufils, V.Vie, G.Paboeuf, B.Broadhurst, F.Schweisguth, T.L.Blundell, V.M.Bolanos-Garcia. Crystal Structure, Biochemical and Biophysical Characterisation of NHR1 Domain of E3 Ubiquitin Ligase Neutralized Advances in Enzyme Research V. 1 61 2013.
DOI: 10.4236/AER.2013.13007