Magnesium in PDB 4gzm: Crystal Structure of RAC1 F28L Mutant

All present enzymatic activity of Crystal Structure of RAC1 F28L Mutant:
3.6.5.2;

The structure of Crystal Structure of RAC1 F28L Mutant, PDB code: 4gzm was solved by B.H.Ha, T.J.Boggon, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	27.82 / 2.80
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	40.094, 98.807, 51.994, 90.00, 90.21, 90.00
R / Rfree (%)	25.4 / 28.8

The binding sites of Magnesium atom in the Crystal Structure of RAC1 F28L Mutant (pdb code 4gzm). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of RAC1 F28L Mutant, PDB code: 4gzm:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of RAC1 F28L Mutant


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 RAC1 F28L Mutant within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1001 b:74.2 occ:1.00 O3G A:GSP1000 1.9 0.5 1.0 OG1 A:THR17 2.1 96.8 1.0 OG1 A:THR35 2.2 0.2 1.0 O2B A:GSP1000 2.3 0.9 1.0 CB A:THR35 3.1 0.2 1.0 PG A:GSP1000 3.1 0.9 1.0 O3B A:GSP1000 3.1 0.7 1.0 PB A:GSP1000 3.2 0.2 1.0 OD1 A:ASP57 3.3 0.8 1.0 CB A:THR17 3.5 1.0 1.0 OD2 A:ASP57 3.6 0.8 1.0 N A:THR17 3.8 0.1 1.0 CG A:ASP57 3.9 0.4 1.0 O A:THR58 3.9 0.0 1.0 N A:THR35 4.0 0.3 1.0 CG2 A:THR35 4.1 0.6 1.0 CA A:THR35 4.1 1.0 1.0 O2G A:GSP1000 4.1 0.4 1.0 CA A:THR17 4.1 0.9 1.0 O1B A:GSP1000 4.2 0.7 1.0 O1A A:GSP1000 4.3 0.2 1.0 CG2 A:THR17 4.4 0.3 1.0 CB A:LYS16 4.5 90.9 1.0 O3A A:GSP1000 4.5 0.6 1.0 S1G A:GSP1000 4.5 0.9 1.0 CE A:LYS16 4.6 1.0 1.0 PA A:GSP1000 4.7 0.4 1.0 O2A A:GSP1000 4.8 0.9 1.0 C A:LYS16 4.8 97.3 1.0 NZ A:LYS16 4.9 0.2 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of RAC1 F28L Mutant


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of RAC1 F28L Mutant within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1001 b:74.3 occ:1.00 OG1 B:THR17 2.1 0.2 1.0 OG1 B:THR35 2.1 0.9 1.0 O3G B:GSP1000 2.4 0.1 1.0 O2B B:GSP1000 2.6 0.1 1.0 O2G B:GSP1000 2.7 0.0 1.0 CB B:THR35 2.9 0.3 1.0 OD1 B:ASP57 3.0 0.2 1.0 PG B:GSP1000 3.0 0.9 1.0 OD2 B:ASP57 3.2 0.4 1.0 CG B:ASP57 3.5 0.5 1.0 CB B:THR17 3.5 0.5 1.0 O B:THR58 3.7 0.4 1.0 PB B:GSP1000 3.7 0.2 1.0 O3B B:GSP1000 3.8 0.7 1.0 N B:THR17 3.8 1.0 1.0 CG2 B:THR35 3.9 0.2 1.0 N B:THR35 4.1 0.3 1.0 CA B:THR17 4.1 0.1 1.0 CA B:THR35 4.1 0.1 1.0 CG2 B:THR17 4.4 0.5 1.0 CB B:LYS16 4.4 96.5 1.0 CE B:LYS16 4.5 0.4 1.0 O1A B:GSP1000 4.6 0.6 1.0 O1B B:GSP1000 4.7 0.4 1.0 S1G B:GSP1000 4.7 0.5 1.0 C B:LYS16 4.7 0.1 1.0 NZ B:LYS16 4.9 0.2 1.0 C B:THR58 4.9 0.9 1.0 O3A B:GSP1000 4.9 0.1 1.0

M.J.Davis, B.H.Ha, E.C.Holman, R.Halaban, J.Schlessinger, T.J.Boggon. RAC1P29S Is A Spontaneously Activating Cancer-Associated Gtpase. Proc.Natl.Acad.Sci.Usa V. 110 912 2013.
ISSN: ISSN 0027-8424
PubMed: 23284172
DOI: 10.1073/PNAS.1220895110