Magnesium in PDB 7r4k: Crystal Structure of Human Mitochondrial Nad Kinase

All present enzymatic activity of Crystal Structure of Human Mitochondrial Nad Kinase:
2.7.1.23;

The structure of Crystal Structure of Human Mitochondrial Nad Kinase, PDB code: 7r4k was solved by G.Labesse, C.Mary, M.Gelin, C.Lionne, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.09 / 3.33
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	67.583, 67.583, 221.815, 90, 90, 90
R / Rfree (%)	21.4 / 28.7

The binding sites of Magnesium atom in the Crystal Structure of Human Mitochondrial Nad Kinase (pdb code 7r4k). 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 Human Mitochondrial Nad Kinase, PDB code: 7r4k:

Magnesium binding site 1 out of 1 in the Crystal Structure of Human Mitochondrial Nad Kinase


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 Human Mitochondrial Nad Kinase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg502 b:46.8 occ:1.00 O1A A:NAP501 2.2 51.9 1.0 O A:HOH611 2.2 50.0 1.0 O A:HOH632 2.5 50.9 1.0 O3X A:NAP501 2.7 54.7 1.0 O A:HOH606 2.8 51.4 1.0 O2N A:NAP501 3.0 38.7 1.0 O1N A:NAP501 3.3 50.9 1.0 PA A:NAP501 3.5 50.4 1.0 PN A:NAP501 3.6 54.4 1.0 O2X A:NAP501 3.7 56.6 1.0 P2B A:NAP501 3.8 57.3 1.0 O3 A:NAP501 3.9 53.7 1.0 O A:HOH622 3.9 63.5 1.0 O2A A:NAP501 4.1 46.0 1.0 N A:GLY162 4.2 48.1 1.0 CA A:GLY162 4.5 48.4 1.0 C3B A:NAP501 4.5 57.4 1.0 O3B A:NAP501 4.7 59.2 1.0 C2B A:NAP501 4.7 53.9 1.0 O1X A:NAP501 4.8 60.6 1.0 O5B A:NAP501 4.8 48.0 1.0 O2B A:NAP501 4.9 48.2 1.0

C.Mary, M.H.Soflaee, R.Kesavan, M.Gelin, H.Brown, G.Zacharias, T.P.Mathews, A.Lemoff, C.Lionne, G.Labesse, G.Hoxhaj. Crystal Structure of Human NADK2 Reveals A Dimeric Organization and Active Site Occlusion By Lysine Acetylation. Mol.Cell V. 82 3299 2022.
ISSN: ISSN 1097-2765
PubMed: 35868311
DOI: 10.1016/J.MOLCEL.2022.06.026