Magnesium in PDB 8h47: Blasnase-T13A/P55F

The structure of Blasnase-T13A/P55F, PDB code: 8h47 was solved by F.Lu, W.Wang, H.Chi, T.Ran, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	19.98 / 1.90
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	92.513, 92.513, 230.783, 90, 90, 90
R / Rfree (%)	19.2 / 20.1

The binding sites of Magnesium atom in the Blasnase-T13A/P55F (pdb code 8h47). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 4 binding sites of Magnesium where determined in the Blasnase-T13A/P55F, PDB code: 8h47:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Blasnase-T13A/P55F


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Blasnase-T13A/P55F within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:37.0 occ:0.00 O1 A:FMT403 2.3 36.8 0.0 O A:ASN246 2.5 33.7 1.0 O A:HOH549 2.5 40.8 1.0 OD2 A:ASP250 2.7 42.6 1.0 C A:FMT403 3.2 37.2 0.0 C A:ASN246 3.6 39.5 1.0 CG A:ASP250 3.6 38.2 1.0 NH1 A:ARG223 3.8 34.2 1.0 OD1 A:ASP250 3.9 38.2 1.0 O2 A:FMT403 4.2 37.8 0.0 O A:HOH595 4.3 35.7 1.0 CA A:ASN246 4.3 37.4 1.0 N A:GLY219 4.3 30.9 1.0 CB A:ASN246 4.5 32.5 1.0 CA A:GLY219 4.5 32.1 1.0 N A:MET247 4.6 32.4 1.0 CA A:MET247 4.8 32.9 1.0 N A:ASP250 4.9 33.3 1.0 CB A:ASP250 4.9 33.7 1.0

Magnesium binding site 2 out of 4 in the Blasnase-T13A/P55F


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Blasnase-T13A/P55F within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:33.1 occ:0.00 O A:ASP295 2.3 31.4 1.0 O A:HOH664 2.5 36.2 1.0 O A:HOH560 2.8 31.2 1.0 O A:HOH647 3.0 36.4 1.0 O A:GLU268 3.2 31.6 1.0 C A:ASP295 3.5 31.1 1.0 O A:HOH583 3.5 36.3 1.0 C A:GLU268 4.1 29.3 1.0 CB A:ASP295 4.1 30.4 1.0 N A:ASP297 4.1 28.6 1.0 O A:HOH550 4.1 36.6 1.0 CA A:ASP295 4.2 31.8 1.0 C A:TYR296 4.3 30.0 1.0 O A:ALA267 4.5 31.2 1.0 CD1 A:TYR159 4.5 34.2 1.0 N A:TYR296 4.5 30.9 1.0 CE1 A:TYR159 4.6 34.3 1.0 O A:HOH612 4.6 42.6 1.0 CA A:TYR296 4.7 29.5 1.0 CA A:GLU269 4.8 31.8 1.0 CG A:ASP295 4.8 32.6 1.0 N A:GLU269 4.8 30.6 1.0 CA A:ASP297 4.8 29.6 1.0 O A:TYR296 4.8 31.3 1.0 CA A:GLU268 4.9 31.6 1.0

Magnesium binding site 3 out of 4 in the Blasnase-T13A/P55F


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Blasnase-T13A/P55F within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg401 b:44.7 occ:0.00 O A:HOH619 2.1 42.5 1.0 O B:HOH505 2.5 51.4 1.0 OE1 B:GLU207 2.6 48.9 1.0 OE2 B:GLU207 2.7 43.3 1.0 O B:GLU228 2.9 47.2 1.0 CD B:GLU207 3.0 39.9 1.0 O2 B:FMT408 3.6 42.5 0.0 CB B:GLU228 3.8 42.1 1.0 C B:GLU228 3.9 41.6 1.0 OD2 A:ASP218 4.0 36.1 1.0 CE A:LYS220 4.0 34.6 1.0 O A:HOH640 4.1 49.5 1.0 NZ A:LYS220 4.1 37.3 1.0 C B:FMT408 4.3 42.7 0.0 CA B:GLU228 4.5 41.9 1.0 CG B:GLU207 4.5 42.5 1.0 OE1 B:GLU228 4.7 60.8 1.0 CG B:GLU228 4.7 46.0 1.0 O1 B:FMT408 4.7 44.6 0.0 N B:GLY229 4.9 36.5 1.0

Magnesium binding site 4 out of 4 in the Blasnase-T13A/P55F


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Blasnase-T13A/P55F within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:36.9 occ:0.00 O B:HOH670 2.4 41.5 1.0 O B:ASP295 2.6 32.8 1.0 O B:HOH602 2.6 38.0 1.0 O B:HOH652 2.9 44.2 1.0 O B:GLU268 3.2 33.3 1.0 O B:HOH611 3.5 35.6 1.0 O B:HOH629 3.6 45.1 1.0 C B:ASP295 3.7 36.7 1.0 C B:GLU268 4.0 34.1 1.0 O B:HOH547 4.1 42.1 1.0 N B:ASP297 4.1 31.6 1.0 O B:ALA267 4.2 33.0 1.0 O B:HOH560 4.2 37.4 1.0 CB B:ASP295 4.3 36.0 1.0 C B:TYR296 4.3 33.5 1.0 CA B:ASP295 4.4 35.9 1.0 N B:TYR296 4.6 30.5 1.0 CA B:ASP297 4.7 29.3 1.0 CD1 B:TYR159 4.7 35.3 1.0 CA B:GLU268 4.7 35.5 1.0 N B:GLU269 4.7 32.0 1.0 O B:TYR296 4.7 32.9 1.0 CA B:TYR296 4.8 32.9 1.0 CA B:GLU269 4.8 35.2 1.0 CE1 B:TYR159 4.8 34.2 1.0 CB B:ASP297 4.8 29.2 1.0

F.Lu, W.Wang, H.Chi, T.Ran. Structure-Based Rational Design of Bacillus Licheniformis L-Asparaginase with Low/No D-Asparaginase Activity For A Safer Enzyme To Be Published.