Magnesium in PDB 1zio: Phosphotransferase

All present enzymatic activity of Phosphotransferase:
2.7.4.3;

The structure of Phosphotransferase, PDB code: 1zio was solved by M.B.Berry, G.N.Phillips Jr., with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	10.00 / 1.96
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	41.200, 62.165, 41.930, 90.00, 117.10, 90.00
R / Rfree (%)	16.1 / 22.8

The structure of Phosphotransferase also contains other interesting chemical elements:

Zinc

(Zn)

1 atom

The binding sites of Magnesium atom in the Phosphotransferase (pdb code 1zio). 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 Phosphotransferase, PDB code: 1zio:

Magnesium binding site 1 out of 1 in the Phosphotransferase


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Phosphotransferase within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg220 b:12.8 occ:1.00 O A:HOH302 1.9 5.3 1.0 O A:HOH301 2.1 2.3 0.8 O A:HOH300 2.2 8.1 1.0 O2G A:AP5218 2.2 9.1 1.0 O A:HOH303 2.2 10.4 1.0 O2B A:AP5218 2.2 4.5 1.0 PG A:AP5218 3.3 9.6 1.0 PB A:AP5218 3.4 8.3 1.0 O3B A:AP5218 3.6 15.5 1.0 N A:GLY14 4.1 8.1 1.0 O3G A:AP5218 4.1 11.2 1.0 O2E A:AP5218 4.2 13.0 1.0 O1E A:AP5218 4.2 6.1 1.0 OD2 A:ASP84 4.3 11.2 1.0 O1G A:AP5218 4.3 9.9 1.0 O A:HOH397 4.3 35.4 1.0 O2A A:AP5218 4.3 8.0 1.0 O A:HOH321 4.3 9.7 1.0 O3A A:AP5218 4.4 7.6 1.0 CA A:GLY14 4.4 4.3 1.0 PE A:AP5218 4.4 10.4 1.0 O1B A:AP5218 4.4 6.1 1.0 OD1 A:ASP84 4.5 14.9 1.0 O3D A:AP5218 4.5 14.7 1.0 OD1 A:ASP33 4.8 21.7 1.0 PD A:AP5218 4.8 9.7 1.0 PA A:AP5218 4.8 7.8 1.0 CG A:ASP84 4.8 13.6 1.0 CB A:LYS13 4.9 6.9 1.0

M.B.Berry, G.N.Phillips Jr.. Crystal Structures of Bacillus Stearothermophilus Adenylate Kinase with Bound AP5A, MG2+ AP5A, and MN2+ AP5A Reveal An Intermediate Lid Position and Six Coordinate Octahedral Geometry For Bound MG2+ and MN2+. Proteins V. 32 276 1998.
ISSN: ISSN 0887-3585
PubMed: 9715904
DOI: 10.1002/(SICI)1097-0134(19980815)32:3<276::AID-PROT3>3.0.CO;2-G