Magnesium in PDB 8h45: Blasnase-T13A/P55N

The structure of Blasnase-T13A/P55N, PDB code: 8h45 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)	19.83 / 1.97
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	92.656, 92.656, 230.397, 90, 90, 90
R / Rfree (%)	18.4 / 20.2

The binding sites of Magnesium atom in the Blasnase-T13A/P55N (pdb code 8h45). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 7 binding sites of Magnesium where determined in the Blasnase-T13A/P55N, PDB code: 8h45:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7;

Magnesium binding site 1 out of 7 in the Blasnase-T13A/P55N


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Blasnase-T13A/P55N within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:45.5 occ:0.00 OE2 B:GLU207 2.1 50.1 1.0 O B:HOH666 2.2 47.9 1.0 O1 B:FMT406 2.5 43.4 0.0 C B:FMT406 2.5 43.7 0.0 OD2 A:ASP218 2.5 42.5 1.0 O A:HOH546 2.7 42.3 1.0 CD B:GLU207 3.1 50.1 1.0 MG B:MG401 3.3 47.5 0.0 CG A:ASP218 3.4 41.2 1.0 O2 B:FMT406 3.7 43.3 0.0 OE1 B:GLU207 3.8 54.5 1.0 NZ A:LYS220 3.9 39.6 1.0 CG B:GLU207 4.0 46.1 1.0 CB A:ASP218 4.1 35.6 1.0 OD1 A:ASP218 4.3 41.0 1.0 O B:HOH603 4.4 44.0 1.0 O A:HOH647 4.6 54.8 1.0 O A:HOH566 4.7 39.6 1.0 CE A:LYS220 4.8 39.0 1.0 CB B:GLU207 5.0 43.6 1.0

Magnesium binding site 2 out of 7 in the Blasnase-T13A/P55N


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Blasnase-T13A/P55N within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:56.6 occ:0.00 O A:SER79 2.2 55.5 1.0 OD2 A:ASP81 3.2 62.2 1.0 C A:SER79 3.2 56.6 1.0 CG A:ASP81 3.6 60.9 1.0 OD1 A:ASP81 3.6 57.8 1.0 CA A:SER79 3.8 56.5 1.0 CB A:SER79 4.2 56.7 1.0 N A:TYR80 4.3 55.9 1.0 N A:ASP81 4.3 52.5 1.0 C A:TYR80 4.4 49.2 1.0 CB A:LYS4 4.4 56.6 1.0 N A:LYS4 4.5 54.6 1.0 CA A:TYR80 4.6 52.3 1.0 O A:LYS2 4.8 74.3 1.0 O A:TYR80 4.8 47.7 1.0 CB A:ASP81 4.8 51.0 1.0 CA A:ASP81 4.9 51.3 1.0

Magnesium binding site 3 out of 7 in the Blasnase-T13A/P55N


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Blasnase-T13A/P55N within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:37.7 occ:0.00 O2 A:FMT405 2.1 38.1 0.0 OD2 A:ASP250 2.4 43.0 1.0 O A:HOH545 2.4 41.3 1.0 O A:ASN246 2.6 35.8 1.0 C A:FMT405 3.1 38.5 0.0 CG A:ASP250 3.4 41.1 1.0 OD1 A:ASP250 3.7 41.2 1.0 NH1 A:ARG223 3.7 36.0 1.0 C A:ASN246 3.7 37.1 1.0 N A:GLY219 4.2 33.0 1.0 O1 A:FMT405 4.2 39.4 0.0 CA A:GLY219 4.4 34.7 1.0 O A:HOH576 4.4 38.5 1.0 CA A:ASN246 4.5 37.6 1.0 N A:MET247 4.6 33.6 1.0 CB A:ASN246 4.7 32.8 1.0 CB A:ASP250 4.7 35.4 1.0 CA A:MET247 4.7 34.3 1.0 N A:ASP250 4.8 33.2 1.0 CZ A:ARG223 5.0 40.2 1.0

Magnesium binding site 4 out of 7 in the Blasnase-T13A/P55N


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Blasnase-T13A/P55N within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg404 b:35.0 occ:0.00 O A:HOH612 2.1 45.1 1.0 O A:ASP295 2.6 28.7 1.0 O A:HOH536 2.9 31.8 1.0 O A:GLU268 3.0 35.9 1.0 O A:HOH599 3.3 43.5 1.0 O A:HOH608 3.7 38.7 1.0 C A:ASP295 3.7 31.5 1.0 O A:HOH541 3.9 41.9 1.0 C A:GLU268 3.9 33.4 1.0 CB A:ASP295 4.2 34.5 1.0 N A:ASP297 4.3 29.9 1.0 CD1 A:TYR159 4.3 32.7 1.0 CA A:ASP295 4.4 32.2 1.0 CE1 A:TYR159 4.4 36.3 1.0 O A:HOH613 4.5 39.4 1.0 O A:ALA267 4.5 30.1 1.0 C A:TYR296 4.5 32.7 1.0 N A:GLU269 4.7 32.1 1.0 N A:TYR296 4.7 30.3 1.0 CA A:GLU269 4.7 31.7 1.0 CA A:GLU268 4.7 34.0 1.0 CA A:TYR296 4.8 32.4 1.0 CG A:ASP295 4.8 38.5 1.0 O A:HOH573 4.9 31.7 1.0 CA A:ASP297 4.9 27.1 1.0 O A:TYR296 5.0 32.5 1.0

Magnesium binding site 5 out of 7 in the Blasnase-T13A/P55N


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Blasnase-T13A/P55N within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg401 b:47.5 occ:0.00 O B:HOH666 2.6 47.9 1.0 OE1 B:GLU207 2.7 54.5 1.0 OE2 B:GLU207 2.8 50.1 1.0 O B:GLU228 2.9 52.6 1.0 CD B:GLU207 3.1 50.1 1.0 MG A:MG401 3.3 45.5 0.0 CB B:GLU228 3.7 41.9 1.0 C B:GLU228 3.9 41.0 1.0 OD2 A:ASP218 4.0 42.5 1.0 CE A:LYS220 4.0 39.0 1.0 O A:HOH647 4.1 54.8 1.0 NZ A:LYS220 4.2 39.6 1.0 OE2 B:GLU228 4.4 64.0 1.0 CA B:GLU228 4.4 42.9 1.0 O1 B:FMT406 4.5 43.4 0.0 CG B:GLU207 4.6 46.1 1.0 CG B:GLU228 4.9 42.9 1.0 N B:GLY229 5.0 38.5 1.0

Magnesium binding site 6 out of 7 in the Blasnase-T13A/P55N


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Blasnase-T13A/P55N within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:37.1 occ:0.00 O B:HOH625 2.3 44.4 1.0 O B:HOH538 2.3 37.7 1.0 O B:ASP295 2.6 33.7 1.0 O B:GLU268 2.9 35.1 1.0 O B:HOH637 3.0 40.9 1.0 C B:ASP295 3.6 33.0 1.0 O B:HOH575 3.7 39.5 1.0 C B:GLU268 3.7 36.3 1.0 CB B:ASP295 4.1 37.8 1.0 O B:ALA267 4.1 31.9 1.0 CA B:ASP295 4.2 36.4 1.0 O B:HOH548 4.3 39.9 1.0 N B:ASP297 4.3 29.9 1.0 N B:GLU269 4.4 32.3 1.0 CA B:GLU269 4.5 36.6 1.0 C B:TYR296 4.6 32.8 1.0 CA B:GLU268 4.6 37.6 1.0 O B:GLY270 4.7 39.6 1.0 N B:TYR296 4.7 32.3 1.0 CD1 B:TYR159 4.7 34.7 1.0 CE1 B:TYR159 4.8 37.0 1.0 CG B:ASP295 4.9 41.3 1.0 CA B:TYR296 5.0 31.5 1.0 O B:TYR296 5.0 33.5 1.0 C B:GLU269 5.0 35.6 1.0

Magnesium binding site 7 out of 7 in the Blasnase-T13A/P55N


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of Blasnase-T13A/P55N within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg403 b:40.8 occ:0.00 O1 B:FMT405 2.3 40.9 0.0 OD2 B:ASP250 2.5 45.8 1.0 O B:HOH613 2.5 46.7 1.0 O B:ASN246 2.6 38.5 1.0 C B:FMT405 3.3 41.1 0.0 CG B:ASP250 3.4 42.6 1.0 C B:ASN246 3.7 39.2 1.0 OD1 B:ASP250 3.8 45.5 1.0 O B:HOH533 3.9 43.8 1.0 N B:ASP250 4.2 39.3 1.0 O2 B:FMT405 4.3 41.2 0.0 NH1 B:ARG223 4.4 39.2 1.0 CA B:ASN246 4.5 38.1 1.0 N B:MET247 4.5 36.5 1.0 N B:GLY249 4.6 43.1 1.0 CB B:ASP250 4.6 37.7 1.0 CA B:GLY249 4.6 41.9 1.0 CA B:MET247 4.7 35.9 1.0 N B:GLY219 4.8 37.9 1.0 C B:MET247 4.8 36.8 1.0 C B:GLY249 4.8 38.5 1.0 CB B:ASN246 4.9 38.0 1.0 CA B:GLY219 4.9 36.0 1.0 CA B:ASP250 5.0 34.6 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.