Magnesium in PDB 3wjr: Crystal Structure of Hype in Complex with A Nucleotide

The structure of Crystal Structure of Hype in Complex with A Nucleotide, PDB code: 3wjr was solved by T.Tominaga, S.Watanabe, K.Miki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.00 / 1.86
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	102.657, 102.657, 105.728, 90.00, 90.00, 90.00
R / Rfree (%)	17.3 / 20

The binding sites of Magnesium atom in the Crystal Structure of Hype in Complex with A Nucleotide (pdb code 3wjr). 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 Hype in Complex with A Nucleotide, PDB code: 3wjr:

Magnesium binding site 1 out of 1 in the Crystal Structure of Hype in Complex with A Nucleotide


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 Hype in Complex with A Nucleotide within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg412 b:46.8 occ:1.00 OD1 A:ASP43 2.4 32.8 1.0 OD1 A:ASP84 2.6 33.5 1.0 O A:HOH652 2.9 41.3 1.0 CG A:ASP43 3.4 29.9 1.0 CG A:ASP84 3.4 34.3 1.0 CB A:ASP43 3.6 19.2 1.0 CB A:ASP221 3.7 29.9 1.0 O A:HOH542 3.7 43.9 1.0 OD2 A:ASP84 3.8 38.8 1.0 CA A:ASP43 3.9 22.5 1.0 O A:ASP221 4.1 28.7 1.0 O2P A:AMP403 4.3 57.7 0.7 OD2 A:ASP221 4.3 29.0 1.0 O A:HOH653 4.4 48.8 1.0 CG A:ASP221 4.5 36.2 1.0 OG1 A:THR223 4.5 38.5 1.0 CB A:ASP84 4.5 18.9 1.0 OD2 A:ASP43 4.5 29.6 1.0 O A:ASP43 4.5 21.0 1.0 N A:ASP221 4.6 23.9 1.0 CA A:ASP221 4.7 30.6 1.0 O A:HOH525 4.7 31.9 1.0 C A:ASP43 4.7 26.2 1.0 C A:ASP221 4.8 26.6 1.0 CA A:ASP84 4.9 18.6 1.0 N A:ASP43 5.0 21.1 1.0

T.Tominaga, S.Watanabe, R.Matsumi, H.Atomi, T.Imanaka, K.Miki. Crystal Structures of the Carbamoylated and Cyanated Forms of Hype For [Nife] Hydrogenase Maturation Proc.Natl.Acad.Sci.Usa V. 110 20485 2013.
ISSN: ISSN 0027-8424
PubMed: 24297906
DOI: 10.1073/PNAS.1313620110