Magnesium in PDB 2itn: Crystal Structure of Egfr Kinase Domain G719S Mutation in Complex with Amp-Pnp

All present enzymatic activity of Crystal Structure of Egfr Kinase Domain G719S Mutation in Complex with Amp-Pnp:
2.7.10.1;

The structure of Crystal Structure of Egfr Kinase Domain G719S Mutation in Complex with Amp-Pnp, PDB code: 2itn was solved by C.-H.Yun, T.J.Boggon, Y.Li, S.Woo, H.Greulich, M.Meyerson, M.J.Eck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	24.95 / 2.47
Space group	I 2 3
Cell size a, b, c (Å), α, β, γ (°)	145.481, 145.481, 145.481, 90.00, 90.00, 90.00
R / Rfree (%)	19.7 / 26.7

The binding sites of Magnesium atom in the Crystal Structure of Egfr Kinase Domain G719S Mutation in Complex with Amp-Pnp (pdb code 2itn). 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 Egfr Kinase Domain G719S Mutation in Complex with Amp-Pnp, PDB code: 2itn:

Magnesium binding site 1 out of 1 in the Crystal Structure of Egfr Kinase Domain G719S Mutation in Complex with Amp-Pnp


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 Egfr Kinase Domain G719S Mutation in Complex with Amp-Pnp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg2020 b:0.8 occ:1.00 O1G A:ANP2021 2.8 0.3 1.0 O2G A:ANP2021 3.1 0.7 1.0 N3B A:ANP2021 3.1 0.0 1.0 PG A:ANP2021 3.2 0.5 1.0 OD1 A:ASP855 3.3 49.6 1.0 O A:HOH3079 3.6 67.0 1.0 OD2 A:ASP855 3.6 48.0 1.0 CG A:ASP855 3.8 45.8 1.0 NZ A:LYS745 4.0 60.2 1.0 OE1 A:GLU762 4.2 59.4 1.0 O A:HOH3069 4.6 68.0 1.0 PB A:ANP2021 4.7 0.1 1.0 O3G A:ANP2021 4.7 1.0 1.0

C.-H.Yun, T.J.Boggon, Y.Li, S.Woo, H.Greulich, M.Meyerson, M.J.Eck. Structures of Lung Cancer-Derived Egfr Mutants and Inhibitor Complexes: Mechanism of Activation and Insights Into Differential Inhibitor Sensitivity Cancer Cell V. 11 217 2007.
ISSN: ISSN 1535-6108
PubMed: 17349580
DOI: 10.1016/J.CCR.2006.12.017