Magnesium in PDB 8afc: Crystal Structure of Kras-G12C in Complex with Compound 12

All present enzymatic activity of Crystal Structure of Kras-G12C in Complex with Compound 12:
3.6.5.2;

The structure of Crystal Structure of Kras-G12C in Complex with Compound 12, PDB code: 8afc was solved by J.Boettcher, D.Kessler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	68.02 / 2.41
Space group	P 63 2 2
Cell size a, b, c (Å), α, β, γ (°)	136.04, 136.04, 91.26, 90, 90, 120
R / Rfree (%)	21.1 / 26.6

The binding sites of Magnesium atom in the Crystal Structure of Kras-G12C in Complex with Compound 12 (pdb code 8afc). 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 Kras-G12C in Complex with Compound 12, PDB code: 8afc:

Magnesium binding site 1 out of 1 in the Crystal Structure of Kras-G12C in Complex with Compound 12


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 Kras-G12C in Complex with Compound 12 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg202 b:47.4 occ:1.00 O A:HOH311 1.9 45.4 1.0 O1B A:GDP201 2.0 46.4 1.0 O A:HOH304 2.1 46.2 1.0 OG A:SER17 2.1 44.9 1.0 O A:HOH310 2.1 39.4 1.0 O A:HOH302 2.3 48.8 1.0 CB A:SER17 3.2 44.0 1.0 PB A:GDP201 3.2 49.3 1.0 O2B A:GDP201 3.5 43.6 1.0 N A:SER17 3.9 44.3 1.0 O A:ASP33 4.0 55.9 1.0 O2A A:GDP201 4.0 45.9 1.0 CA A:SER17 4.1 44.3 1.0 OD2 A:ASP57 4.1 69.1 1.0 O3A A:GDP201 4.2 55.3 1.0 O A:PRO34 4.2 56.9 1.0 CD2 A:TYR32 4.3 68.7 1.0 O3B A:GDP201 4.3 49.8 1.0 OD1 A:ASP57 4.3 63.2 1.0 CA A:PRO34 4.4 50.8 1.0 C A:PRO34 4.6 55.6 1.0 PA A:GDP201 4.6 45.5 1.0 O A:ILE36 4.6 51.4 1.0 CB A:ALA59 4.7 45.8 1.0 CE2 A:TYR32 4.7 70.2 1.0 CG A:ASP57 4.7 63.3 1.0 O1A A:GDP201 4.7 48.8 1.0 O A:THR58 4.7 50.3 1.0 CE A:LYS16 4.8 43.1 1.0 CB A:LYS16 4.9 46.8 1.0 C A:ASP33 4.9 56.1 1.0 O A:HOH309 5.0 45.8 1.0

J.Broker, A.G.Waterson, C.Smethurst, D.Kessler, J.Bottcher, M.Mayer, G.Gmaschitz, J.Phan, A.Little, J.R.Abbott, Q.Sun, M.Gmachl, D.Rudolph, H.Arnhof, K.Rumpel, F.Savarese, T.Gerstberger, N.Mischerikow, M.Treu, L.Herdeis, T.Wunberg, A.Gollner, H.Weinstabl, A.Mantoulidis, O.Kramer, D.B.Mcconnell, S.W Fesik. Fragment Optimization of Reversible Binding to the Switch II Pocket on Kras Leads to A Potent, in Vivo Active Kras G12C Inhibitor. J.Med.Chem. V. 65 14614 2022.
ISSN: ISSN 0022-2623
PubMed: 36300829
DOI: 10.1021/ACS.JMEDCHEM.2C01120