Aluminium 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
Magnesium	(Mg)	2 atoms

The binding sites of Aluminium 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 Aluminium atom.
In total 2 binding sites of Aluminium 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 Aluminium binding site number: 1; 2;

Aluminium 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 Aluminium with other atoms in the Al 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:Al203 b:25.6 occ:1.00 AL B:ALF203 0.0 25.6 1.0 F4 B:ALF203 1.8 25.8 1.0 F3 B:ALF203 1.8 26.7 1.0 F2 B:ALF203 1.8 27.6 1.0 F1 B:ALF203 1.8 24.9 1.0 O B:HOH303 1.8 25.7 1.0 O3B B:GDP202 2.1 33.1 1.0 MG B:MG201 3.3 28.4 1.0 PB B:GDP202 3.3 31.8 1.0 O1B B:GDP202 3.7 30.4 1.0 O B:HOH317 3.7 30.2 1.0 N B:GLY62 3.7 30.8 1.0 NE2 B:GLN63 3.8 30.6 1.0 NZ B:LYS18 3.8 33.2 1.0 N B:THR37 4.0 29.7 1.0 OE1 B:GLN63 4.0 30.9 1.0 N B:ALA15 4.1 31.2 1.0 CD B:GLN63 4.3 30.7 1.0 O2B B:GDP202 4.3 33.0 1.0 OH B:TYR34 4.4 31.1 1.0 O3A B:GDP202 4.4 32.4 1.0 O B:THR37 4.4 28.9 1.0 CA B:GLY62 4.5 31.2 1.0 O B:HOH309 4.5 27.8 1.0 CA B:ALA61 4.5 31.9 1.0 CA B:PRO36 4.5 30.4 1.0 CB B:THR37 4.6 29.5 1.0 OG1 B:THR37 4.6 30.6 1.0 CE B:LYS18 4.6 34.1 1.0 C B:ALA61 4.7 31.5 1.0 CA B:THR37 4.8 29.9 1.0 C B:PRO36 4.8 29.9 1.0 CA B:ALA15 4.8 31.9 1.0 O B:THR60 4.8 29.9 1.0 CA B:GLY14 4.9 32.1 1.0 CB B:PRO36 5.0 30.3 1.0 CE1 B:TYR34 5.0 31.1 1.0

Aluminium 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 Aluminium with other atoms in the Al 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:Al203 b:26.3 occ:1.00 AL G:ALF203 0.0 26.3 1.0 F2 G:ALF203 1.8 25.6 1.0 F1 G:ALF203 1.8 25.7 1.0 F4 G:ALF203 1.8 27.0 1.0 F3 G:ALF203 1.8 22.2 1.0 O G:HOH303 1.8 24.3 1.0 O3B G:GDP202 2.2 33.6 1.0 PB G:GDP202 3.4 31.8 1.0 MG G:MG201 3.6 28.5 1.0 N G:GLY62 3.7 28.9 1.0 NZ G:LYS18 3.7 30.6 1.0 O2B G:GDP202 3.8 29.4 1.0 O G:HOH305 3.8 27.4 1.0 NE2 G:GLN63 3.8 30.9 1.0 OE1 G:GLN63 3.8 31.0 1.0 N G:ALA15 4.0 33.9 1.0 N G:THR37 4.1 31.5 1.0 O1B G:GDP202 4.1 31.5 1.0 CD G:GLN63 4.2 30.5 1.0 OH G:TYR34 4.4 31.7 1.0 CA G:GLY62 4.4 29.5 1.0 O G:THR37 4.5 32.4 1.0 CE G:LYS18 4.6 31.0 1.0 CA G:ALA61 4.6 30.3 1.0 O3A G:GDP202 4.6 32.7 1.0 O G:THR60 4.6 31.9 1.0 CA G:PRO36 4.6 31.9 1.0 C G:ALA61 4.6 30.1 1.0 CB G:THR37 4.7 31.4 1.0 CA G:ALA15 4.7 34.6 1.0 OG1 G:THR37 4.7 30.7 1.0 CA G:GLY14 4.7 31.7 1.0 C G:PRO36 4.9 32.0 1.0 CA G:THR37 4.9 31.9 1.0 C G:GLY14 4.9 32.8 1.0 O G:HOH306 5.0 28.0 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