Magnesium in PDB 8fg3: Hras R97L Crystal Form 2

All present enzymatic activity of Hras R97L Crystal Form 2:
3.6.5.2;

The structure of Hras R97L Crystal Form 2, PDB code: 8fg3 was solved by S.Fetics, C.W.Johnson, C.Mattos, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	28.74 / 1.49
Space group	P 32 2 1
Cell size a, b, c (Å), α, β, γ (°)	39.65, 39.65, 157.616, 90, 90, 120
R / Rfree (%)	20.6 / 24.7

The binding sites of Magnesium atom in the Hras R97L Crystal Form 2 (pdb code 8fg3). 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 Hras R97L Crystal Form 2, PDB code: 8fg3:

Magnesium binding site 1 out of 1 in the Hras R97L Crystal Form 2


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Hras R97L Crystal Form 2 within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg202 b:12.8 occ:1.00 O2G A:GNP201 2.0 14.6 1.0 O A:HOH340 2.1 12.0 1.0 O2B A:GNP201 2.1 11.7 1.0 O A:HOH352 2.1 15.1 1.0 OG A:SER17 2.1 11.9 1.0 OG1 A:THR35 2.1 15.2 1.0 CB A:THR35 3.1 16.9 1.0 CB A:SER17 3.1 9.9 1.0 PG A:GNP201 3.2 12.9 1.0 PB A:GNP201 3.2 11.2 1.0 N3B A:GNP201 3.4 11.9 1.0 N A:THR35 3.8 17.4 1.0 N A:SER17 3.9 11.2 1.0 OD2 A:ASP57 4.1 16.1 1.0 CA A:THR35 4.1 17.2 1.0 CA A:SER17 4.1 10.3 1.0 O2A A:GNP201 4.1 15.5 1.0 O3G A:GNP201 4.1 14.8 1.0 OD1 A:ASP57 4.2 14.1 1.0 CG2 A:THR35 4.2 19.1 1.0 O A:HOH369 4.3 29.8 1.0 O1B A:GNP201 4.3 12.1 1.0 O3A A:GNP201 4.3 11.5 1.0 O A:THR58 4.3 16.6 1.0 O1G A:GNP201 4.3 13.2 1.0 O A:ASP33 4.4 19.4 1.0 CG A:ASP57 4.5 16.4 1.0 PA A:GNP201 4.6 12.5 1.0 O1A A:GNP201 4.6 12.2 1.0 C A:PRO34 4.7 21.8 1.0 CB A:LYS16 4.8 9.6 1.0 C A:LYS16 4.9 9.5 1.0 CE A:LYS16 5.0 12.3 1.0 CA A:PRO34 5.0 19.1 1.0

C.W.Johnson, S.K.Fetics, K.P.Davis, J.A.Rodrigues, C.Mattos. Allosteric Site Variants Affect Gtp Hydrolysis on Ras. Protein Sci. E4767 2023.
ISSN: ESSN 1469-896X
PubMed: 37615343
DOI: 10.1002/PRO.4767