Magnesium in PDB 8afb: Crystal Structure of Kras-G12C in Complex with Compound 23 (Bi-0474)

All present enzymatic activity of Crystal Structure of Kras-G12C in Complex with Compound 23 (Bi-0474):
3.6.5.2;

The structure of Crystal Structure of Kras-G12C in Complex with Compound 23 (Bi-0474), PDB code: 8afb 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)	40.00 / 1.12
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	68.675, 40.513, 56.472, 90, 95.67, 90
R / Rfree (%)	20.2 / 22.2

The binding sites of Magnesium atom in the Crystal Structure of Kras-G12C in Complex with Compound 23 (Bi-0474) (pdb code 8afb). 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 23 (Bi-0474), PDB code: 8afb:

Magnesium binding site 1 out of 1 in the Crystal Structure of Kras-G12C in Complex with Compound 23 (Bi-0474)


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 23 (Bi-0474) within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg202 b:6.5 occ:1.00 O A:HOH308 2.0 7.6 1.0 O1B A:GDP201 2.1 6.5 1.0 O A:HOH324 2.1 7.4 1.0 OG A:SER17 2.1 6.4 1.0 O A:HOH356 2.1 7.4 1.0 O A:HOH304 2.1 6.7 1.0 CB A:SER17 3.2 6.4 1.0 PB A:GDP201 3.3 6.9 1.0 O2B A:GDP201 3.5 7.7 1.0 N A:SER17 3.9 6.0 1.0 CA A:SER17 4.1 5.2 1.0 OD2 A:ASP57 4.1 8.9 1.0 O2A A:GDP201 4.1 8.3 1.0 OD1 A:ASP57 4.2 9.4 1.0 O3A A:GDP201 4.3 7.4 1.0 CA A:PRO34 4.3 8.5 1.0 O A:ASP33 4.3 8.4 1.0 O A:PRO34 4.3 10.7 1.0 O3B A:GDP201 4.4 6.4 1.0 O A:ILE36 4.5 9.0 1.0 O A:THR58 4.6 8.9 1.0 CG A:ASP57 4.6 8.1 1.0 PA A:GDP201 4.6 7.2 1.0 C A:PRO34 4.6 11.1 1.0 O1A A:GDP201 4.8 8.0 1.0 CD2 A:TYR32 4.8 7.9 1.0 O A:TYR32 4.8 9.0 1.0 CB A:LYS16 4.8 7.0 0.5 CB A:LYS16 4.9 7.0 0.5 C A:LYS16 5.0 7.4 1.0 CE A:LYS16 5.0 4.7 0.5

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