Magnesium in PDB 6v5l: The Haddock Structure Model of Gdp Kras in Complex with Its Allosteric Inhibitor E22

The binding sites of Magnesium atom in the The Haddock Structure Model of Gdp Kras in Complex with Its Allosteric Inhibitor E22 (pdb code 6v5l). 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 The Haddock Structure Model of Gdp Kras in Complex with Its Allosteric Inhibitor E22, PDB code: 6v5l:

Magnesium binding site 1 out of 1 in the The Haddock Structure Model of Gdp Kras in Complex with Its Allosteric Inhibitor E22


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of The Haddock Structure Model of Gdp Kras in Complex with Its Allosteric Inhibitor E22 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg202 b:0.5 occ:1.00 OD2 A:ASP57 1.6 0.4 1.0 OD1 A:ASP57 1.7 0.4 1.0 OG A:SER17 1.7 0.4 1.0 CG A:ASP57 1.9 0.4 1.0 HG A:SER17 2.3 0.9 1.0 CB A:SER17 2.8 0.4 1.0 HB3 A:SER17 3.0 0.5 1.0 H A:SER17 3.1 0.4 1.0 O3B A:GDP201 3.2 0.4 1.0 HA A:SER17 3.2 0.4 1.0 CA A:SER17 3.3 0.4 1.0 N A:SER17 3.4 0.4 1.0 CB A:ASP57 3.4 0.3 1.0 HB2 A:LYS16 3.6 0.7 1.0 HB2 A:SER17 3.6 0.4 1.0 O A:THR58 3.7 0.5 1.0 O A:ILE36 3.8 0.5 1.0 HB3 A:ASP57 3.9 0.4 1.0 HB2 A:ASP57 3.9 0.3 1.0 O A:ASP57 4.0 0.4 1.0 C A:ASP57 4.1 0.4 1.0 CA A:ASP57 4.3 0.3 1.0 HE2 A:TYR32 4.3 0.5 1.0 HD2 A:TYR32 4.4 0.5 1.0 HA A:ALA59 4.4 0.4 1.0 C A:LYS16 4.4 0.5 1.0 HB3 A:LYS16 4.5 0.8 1.0 HA A:PRO34 4.5 0.4 1.0 HA A:ASP57 4.5 0.4 1.0 CB A:LYS16 4.5 0.5 1.0 HE3 A:LYS16 4.5 1.3 1.0 C A:THR58 4.5 0.4 1.0 PB A:GDP201 4.6 0.4 1.0 O A:ASP33 4.7 0.4 1.0 N A:THR58 4.7 0.4 1.0 O1B A:GDP201 4.8 0.5 1.0 C A:SER17 4.8 0.4 1.0 HA A:GLU37 4.9 0.5 1.0 C A:ILE36 5.0 0.5 1.0

A.K.Gupta, X.Wang, C.V.Pagba, P.Prakash, J.P.Putkey, A.A.Gorfe. Multi Target Ensemble Based Virtual Screening Yields Novel Allosteric Kras Inhibitors at High Success Rate Chemical Biology & Drug V. 94 1441 2019DESIGN.
PubMed: 30903639
DOI: 10.1111/CBDD