Magnesium in PDB 5m70: Crystal Structure of Human Rhogap Mutated in Its Arginin Finger (R85A) in Complex with Rhoa.Gdp.ALF4- Human

The structure of Crystal Structure of Human Rhogap Mutated in Its Arginin Finger (R85A) in Complex with Rhoa.Gdp.ALF4- Human, PDB code: 5m70 was solved by E.Pellegrini, M.W.Bowler, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	20.00 / 2.20
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	72.554, 66.063, 76.759, 90.00, 96.07, 90.00
R / Rfree (%)	23.8 / 27.7

The structure of Crystal Structure of Human Rhogap Mutated in Its Arginin Finger (R85A) in Complex with Rhoa.Gdp.ALF4- Human also contains other interesting chemical elements:

Fluorine	(F)	8 atoms
Aluminium	(Al)	2 atoms

The binding sites of Magnesium atom in the Crystal Structure of Human Rhogap Mutated in Its Arginin Finger (R85A) in Complex with Rhoa.Gdp.ALF4- Human (pdb code 5m70). 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 Human Rhogap Mutated in Its Arginin Finger (R85A) in Complex with Rhoa.Gdp.ALF4- Human, PDB code: 5m70:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of Human Rhogap Mutated in Its Arginin Finger (R85A) in Complex with Rhoa.Gdp.ALF4- Human


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 Human Rhogap Mutated in Its Arginin Finger (R85A) in Complex with Rhoa.Gdp.ALF4- Human within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg201 b:28.4 occ:1.00 F3 B:ALF203 2.0 26.7 1.0 O B:HOH317 2.2 30.2 1.0 O1B B:GDP202 2.2 30.4 1.0 OG1 B:THR19 2.2 31.3 1.0 O B:HOH309 2.2 27.8 1.0 OG1 B:THR37 2.2 30.6 1.0 CB B:THR37 3.1 29.5 1.0 F2 B:ALF203 3.2 27.6 1.0 CB B:THR19 3.3 32.5 1.0 PB B:GDP202 3.3 31.8 1.0 AL B:ALF203 3.3 25.6 1.0 O3B B:GDP202 3.4 33.1 1.0 N B:THR37 3.7 29.7 1.0 OD2 B:ASP59 3.9 35.7 1.0 CA B:THR37 4.0 29.9 1.0 O2A B:GDP202 4.1 33.7 1.0 O3A B:GDP202 4.1 32.4 1.0 N B:THR19 4.2 34.1 1.0 F1 B:ALF203 4.2 24.9 1.0 CA B:THR19 4.2 33.4 1.0 CG2 B:THR37 4.2 29.2 1.0 CG2 B:THR19 4.3 32.9 1.0 O B:HOH303 4.3 25.7 1.0 O B:HOH302 4.4 25.1 1.0 O2B B:GDP202 4.5 33.0 1.0 O B:VAL35 4.5 32.3 1.0 PA B:GDP202 4.5 32.0 1.0 OD1 B:ASP59 4.6 33.7 1.0 CG B:ASP59 4.6 33.5 1.0 O1A B:GDP202 4.7 33.0 1.0 C B:PRO36 4.8 29.9 1.0 F4 B:ALF203 4.9 25.8 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of Human Rhogap Mutated in Its Arginin Finger (R85A) in Complex with Rhoa.Gdp.ALF4- Human


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 Human Rhogap Mutated in Its Arginin Finger (R85A) in Complex with Rhoa.Gdp.ALF4- Human within 5.0Å range: probe atom residue distance (Å) B Occ G:Mg201 b:28.5 occ:1.00 F2 G:ALF203 2.0 25.6 1.0 O G:HOH306 2.2 28.0 1.0 OG1 G:THR19 2.2 30.4 1.0 O G:HOH305 2.2 27.4 1.0 O2B G:GDP202 2.2 29.4 1.0 OG1 G:THR37 2.2 30.7 1.0 CB G:THR19 3.0 30.4 1.0 CB G:THR37 3.2 31.4 1.0 PB G:GDP202 3.3 31.8 1.0 O3B G:GDP202 3.4 33.6 1.0 AL G:ALF203 3.6 26.3 1.0 F4 G:ALF203 3.6 27.0 1.0 N G:THR37 3.7 31.5 1.0 O2A G:GDP202 3.8 33.5 1.0 CG2 G:THR19 4.0 30.4 1.0 CA G:THR37 4.0 31.9 1.0 N G:THR19 4.1 31.2 1.0 CA G:THR19 4.1 31.1 1.0 O3A G:GDP202 4.2 32.7 1.0 O G:HOH304 4.2 30.7 1.0 O G:VAL35 4.3 33.2 1.0 OD2 G:ASP59 4.3 33.7 1.0 F3 G:ALF203 4.3 22.2 1.0 CG2 G:THR37 4.3 31.7 1.0 PA G:GDP202 4.4 32.3 1.0 O1B G:GDP202 4.5 31.5 1.0 O G:HOH303 4.5 24.3 1.0 OD1 G:ASP59 4.6 33.5 1.0 O1A G:GDP202 4.6 33.2 1.0 C G:PRO36 4.7 32.0 1.0 CG G:ASP59 4.8 32.8 1.0 O G:HOH302 4.9 34.7 1.0

Y.Jin, R.W.Molt, E.Pellegrini, M.J.Cliff, M.W.Bowler, N.G.J.Richards, G.M.Blackburn, J.P.Waltho. Assessing the Influence of Mutation on Gtpase Transition States By Using X-Ray Crystallography, (19) F uc(Nmr), and Dft Approaches. Angew. Chem. Int. Ed. Engl. V. 56 9732 2017.
ISSN: ESSN 1521-3773
PubMed: 28498638
DOI: 10.1002/ANIE.201703074