Magnesium in PDB 8icd: Regulation of An Enzyme By Phosphorylation at the Active Site

All present enzymatic activity of Regulation of An Enzyme By Phosphorylation at the Active Site:
1.1.1.42;

The structure of Regulation of An Enzyme By Phosphorylation at the Active Site, PDB code: 8icd was solved by J.H.Hurley, A.M.Dean, J.L.Sohl, D.E.Koshlandjunior, R.M.Stroud, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	N/A / 2.50
Space group	P 43 21 2
Cell size a, b, c (Å), α, β, γ (°)	105.100, 105.100, 150.300, 90.00, 90.00, 90.00
R / Rfree (%)	16.8 / n/a

The binding sites of Magnesium atom in the Regulation of An Enzyme By Phosphorylation at the Active Site (pdb code 8icd). 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 Regulation of An Enzyme By Phosphorylation at the Active Site, PDB code: 8icd:

Magnesium binding site 1 out of 1 in the Regulation of An Enzyme By Phosphorylation at the Active Site


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Regulation of An Enzyme By Phosphorylation at the Active Site within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg417 b:29.9 occ:1.00 O A:HOH445 2.0 27.5 1.0 O7 A:ICT418 2.0 35.0 1.0 OD2 A:ASP307 2.2 21.4 1.0 O A:HOH482 2.2 37.6 1.0 O2 A:ICT418 2.4 39.3 1.0 C2 A:ICT418 3.0 37.2 1.0 C1 A:ICT418 3.0 37.9 1.0 CG A:ASP307 3.2 22.3 1.0 OD1 A:ASP307 3.6 25.5 1.0 OD1 A:ASP311 3.7 19.7 1.0 O A:ASP307 4.1 18.9 1.0 O6 A:ICT418 4.1 41.6 1.0 C3 A:ICT418 4.1 41.0 1.0 C6 A:ICT418 4.1 41.6 1.0 O1 A:ICT418 4.2 42.0 1.0 CG A:ASP311 4.2 20.9 1.0 OD2 A:ASP311 4.3 28.0 1.0 NH2 A:ARG129 4.3 30.0 1.0 CB A:ASP307 4.4 17.8 1.0 CA A:ASP307 4.5 18.6 1.0 C A:ASP307 4.5 19.5 1.0 NH2 A:ARG153 4.6 22.2 1.0 O5 A:ICT418 4.7 39.0 1.0 O A:HOH481 4.9 34.5 1.0 C4 A:ICT418 5.0 44.8 1.0

J.H.Hurley, A.M.Dean, J.L.Sohl, D.E.Koshland, R.M.Stroud. Regulation of An Enzyme By Phosphorylation at the Active Site. Science V. 249 1012 1990.
ISSN: ISSN 0036-8075
PubMed: 2204109