Magnesium in PDB 8jgq: Crystal Structure of Deinococcus Radiodurans Exopolyphosphatase Complexed with P5

The structure of Crystal Structure of Deinococcus Radiodurans Exopolyphosphatase Complexed with P5, PDB code: 8jgq was solved by Y.Zhao, S.Dai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.88 / 2.50
Space group	P 61
Cell size a, b, c (Å), α, β, γ (°)	166.71, 166.71, 39.3, 90, 90, 120
R / Rfree (%)	21.2 / 24.8

The binding sites of Magnesium atom in the Crystal Structure of Deinococcus Radiodurans Exopolyphosphatase Complexed with P5 (pdb code 8jgq). 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 Deinococcus Radiodurans Exopolyphosphatase Complexed with P5, PDB code: 8jgq:

Magnesium binding site 1 out of 1 in the Crystal Structure of Deinococcus Radiodurans Exopolyphosphatase Complexed with P5


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 Deinococcus Radiodurans Exopolyphosphatase Complexed with P5 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg608 b:61.7 occ:1.00 OD1 A:ASP453 1.8 69.0 1.0 OE2 A:GLU378 2.2 68.8 1.0 NE2 A:HIS340 2.2 56.6 1.0 NE2 A:HIS377 2.2 63.7 1.0 CG A:ASP453 2.6 63.9 1.0 CD2 A:HIS377 2.9 73.3 1.0 CD A:GLU378 2.9 72.3 1.0 OD2 A:ASP453 3.0 64.9 1.0 CD2 A:HIS340 3.1 57.0 1.0 CE1 A:HIS340 3.2 55.1 1.0 CE1 A:HIS377 3.4 63.8 1.0 CG A:GLU378 3.4 67.5 1.0 OE1 A:GLU378 3.7 88.3 1.0 CB A:ASP453 3.9 55.9 1.0 CG A:HIS377 4.1 73.9 1.0 CG A:HIS340 4.3 55.0 1.0 ND1 A:HIS377 4.3 71.9 1.0 ND1 A:HIS340 4.3 53.8 1.0 CG2 A:VAL344 4.6 49.5 1.0 CA A:ASP453 4.7 52.7 1.0 CB A:GLU378 4.8 66.7 1.0 O A:ASP453 4.9 51.1 1.0

S.Dai, B.Wang, R.Ye, D.Zhang, Z.Xie, N.Yu, C.Cai, C.Huang, J.Zhao, F.Zhang, Y.Hua, Y.Zhao, R.Zhou, B.Tian. Structural Evolution of Bacterial Polyphosphate Degradation Enzyme For Phosphorus Cycling. Adv Sci 09602 2024.
ISSN: ESSN 2198-3844
PubMed: 38682481
DOI: 10.1002/ADVS.202309602