Magnesium in PDB 3pls: Ron in Complex with Ligand Amp-Pnp

All present enzymatic activity of Ron in Complex with Ligand Amp-Pnp:
2.7.10.1;

The structure of Ron in Complex with Ligand Amp-Pnp, PDB code: 3pls was solved by J.Wang, S.Steinbacher, M.Augustin, P.Schreiner, D.Epstein, M.J.Mulvihill, A.P.Crew, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.32 / 2.24
Space group	P 41
Cell size a, b, c (Å), α, β, γ (°)	98.631, 98.631, 45.297, 90.00, 90.00, 90.00
R / Rfree (%)	23.1 / 29

The binding sites of Magnesium atom in the Ron in Complex with Ligand Amp-Pnp (pdb code 3pls). 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 Ron in Complex with Ligand Amp-Pnp, PDB code: 3pls:

Magnesium binding site 1 out of 1 in the Ron in Complex with Ligand Amp-Pnp


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Ron in Complex with Ligand Amp-Pnp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1 b:31.4 occ:1.00 O A:HOH1359 1.9 35.4 1.0 OD1 A:ASN1213 2.0 29.9 1.0 O A:HOH33 2.1 43.9 1.0 OD2 A:ASP1226 2.1 34.2 1.0 O1B A:ANP1358 2.5 42.3 1.0 O1A A:ANP1358 2.6 42.3 1.0 CG A:ASN1213 3.0 32.5 1.0 CG A:ASP1226 3.3 25.3 1.0 CA A:ASN1213 3.6 27.0 1.0 PB A:ANP1358 3.7 55.5 1.0 CB A:ASN1213 3.7 26.0 1.0 O A:ARG1212 3.8 34.7 1.0 PA A:ANP1358 3.8 53.1 1.0 ND2 A:ASN1213 4.0 24.2 1.0 CB A:ASP1226 4.0 27.1 1.0 O3A A:ANP1358 4.1 56.5 1.0 N A:ASN1213 4.1 29.4 1.0 N3B A:ANP1358 4.1 65.1 1.0 C A:ARG1212 4.2 30.1 1.0 O5' A:ANP1358 4.3 49.9 1.0 NH2 A:ARG1212 4.3 39.3 1.0 OD1 A:ASP1226 4.3 24.9 1.0 NZ A:LYS1114 4.7 54.4 1.0 CG A:ARG1212 4.9 37.0 1.0 O2B A:ANP1358 4.9 51.6 1.0 C A:ASN1213 5.0 31.4 1.0

J.Wang, S.Steinbacher, M.Augustin, P.Schreiner, D.Epstein, M.J.Mulvihill, A.P.Crew. The Crystal Structure of A Constitutively Active Mutant Ron Kinase Suggests An Intramolecular Autophosphorylation Hypothesis Biochemistry V. 49 7972 2010.
ISSN: ISSN 0006-2960
PubMed: 20726546