Magnesium in PDB 5d41: Egfr Kinase Domain in Complex with Mutant Selective Allosteric Inhibitor

All present enzymatic activity of Egfr Kinase Domain in Complex with Mutant Selective Allosteric Inhibitor:
2.7.10.1;

The structure of Egfr Kinase Domain in Complex with Mutant Selective Allosteric Inhibitor, PDB code: 5d41 was solved by C.-H.Yun, E.Park, M.J.Eck, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	42.24 / 2.31
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	155.133, 72.497, 75.998, 90.00, 113.24, 90.00
R / Rfree (%)	17.4 / 20.7

The binding sites of Magnesium atom in the Egfr Kinase Domain in Complex with Mutant Selective Allosteric Inhibitor (pdb code 5d41). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Egfr Kinase Domain in Complex with Mutant Selective Allosteric Inhibitor, PDB code: 5d41:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Egfr Kinase Domain in Complex with Mutant Selective Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Egfr Kinase Domain in Complex with Mutant Selective Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1101 b:20.4 occ:1.00 O1B A:ANP1102 1.9 19.5 1.0 OD2 A:ASP855 2.0 18.0 1.0 OD1 A:ASN842 2.0 14.3 1.0 O2A A:ANP1102 2.2 17.1 1.0 O A:HOH1212 2.2 34.9 1.0 O A:HOH1304 2.3 34.9 1.0 CG A:ASP855 3.1 14.4 1.0 CG A:ASN842 3.1 15.2 1.0 PB A:ANP1102 3.2 20.5 1.0 PA A:ANP1102 3.3 18.7 1.0 O3A A:ANP1102 3.6 22.3 1.0 ND2 A:ASN842 3.6 15.6 1.0 CB A:ASP855 3.7 19.7 1.0 O1G A:ANP1102 3.7 21.4 1.0 NZ A:LYS745 4.0 27.4 1.0 O5' A:ANP1102 4.0 17.2 1.0 O2B A:ANP1102 4.2 25.2 1.0 OD1 A:ASP855 4.2 18.5 1.0 O A:ARG841 4.3 12.0 1.0 N3B A:ANP1102 4.4 18.7 1.0 CB A:ASN842 4.4 18.0 1.0 PG A:ANP1102 4.4 20.4 1.0 O A:HOH1285 4.4 19.4 1.0 O3G A:ANP1102 4.6 16.7 1.0 O1A A:ANP1102 4.6 25.2 1.0 CA A:ASN842 4.6 22.0 1.0 CG2 A:THR854 4.8 16.2 1.0 C A:ARG841 4.9 16.9 1.0

Magnesium binding site 2 out of 2 in the Egfr Kinase Domain in Complex with Mutant Selective Allosteric Inhibitor


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Egfr Kinase Domain in Complex with Mutant Selective Allosteric Inhibitor within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg2000 b:26.9 occ:1.00 O2B B:ANP2001 1.8 25.7 1.0 OD2 B:ASP855 2.1 23.1 1.0 OD1 B:ASN842 2.1 24.8 1.0 O1A B:ANP2001 2.2 26.2 1.0 O2G B:ANP2001 2.5 45.9 1.0 O B:HOH2192 2.6 24.4 1.0 CG B:ASN842 3.1 23.0 1.0 PB B:ANP2001 3.1 28.2 1.0 PA B:ANP2001 3.2 26.6 1.0 CG B:ASP855 3.2 23.5 1.0 ND2 B:ASN842 3.4 20.7 1.0 O3A B:ANP2001 3.4 35.6 1.0 PG B:ANP2001 3.7 32.5 1.0 NZ B:LYS745 3.9 32.1 1.0 CB B:ASP855 3.9 16.8 1.0 N3B B:ANP2001 3.9 26.7 1.0 O5' B:ANP2001 4.0 32.6 1.0 OD1 B:ASP855 4.2 29.3 1.0 O1G B:ANP2001 4.2 33.5 1.0 O1B B:ANP2001 4.3 34.2 1.0 O B:ARG841 4.4 27.7 1.0 CB B:ASN842 4.5 27.8 1.0 O B:HOH2145 4.5 25.7 1.0 O2A B:ANP2001 4.5 28.3 1.0 CA B:ASN842 4.8 20.4 1.0 O3G B:ANP2001 4.9 43.5 1.0 CG2 B:THR854 4.9 23.5 1.0

Y.Jia, C.H.Yun, E.Park, D.Ercan, M.Manuia, J.Juarez, C.Xu, K.Rhee, T.Chen, H.Zhang, S.Palakurthi, J.Jang, G.Lelais, M.Didonato, B.Bursulaya, P.Y.Michellys, R.Epple, T.H.Marsilje, M.Mcneill, W.Lu, J.Harris, S.Bender, K.K.Wong, P.A.Janne, M.J.Eck. Overcoming Egfr(T790M) and Egfr(C797S) Resistance with Mutant-Selective Allosteric Inhibitors. Nature V. 534 129 2016.
ISSN: ESSN 1476-4687
PubMed: 27251290
DOI: 10.1038/NATURE17960