Magnesium in PDB 8h44: Blasnase-P55N

The structure of Blasnase-P55N, PDB code: 8h44 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)	43.41 / 1.80
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	92.815, 92.815, 231.513, 90, 90, 90
R / Rfree (%)	18.9 / 21.1

The binding sites of Magnesium atom in the Blasnase-P55N (pdb code 8h44). 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-P55N, PDB code: 8h44:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7;

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


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Blasnase-P55N within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:28.9 occ:0.00 O A:HOH558 2.3 27.1 1.0 O A:ASP295 2.5 26.7 1.0 O A:HOH697 2.7 34.6 1.0 O A:GLU268 3.0 29.3 1.0 O A:HOH653 3.0 34.8 1.0 C A:ASP295 3.6 25.7 1.0 C A:GLU268 3.7 30.9 1.0 O A:HOH657 3.9 33.8 1.0 CB A:ASP295 4.0 28.9 1.0 O A:ALA267 4.0 23.6 1.0 O A:HOH575 4.1 42.0 1.0 CA A:ASP295 4.1 25.9 1.0 N A:GLU269 4.3 26.3 1.0 CA A:GLU269 4.4 24.1 1.0 O A:HOH546 4.4 35.2 1.0 N A:ASP297 4.5 24.0 1.0 CA A:GLU268 4.5 30.3 1.0 C A:TYR296 4.6 25.6 1.0 O A:GLY270 4.6 27.3 1.0 N A:TYR296 4.6 26.3 1.0 CG A:ASP295 4.8 29.6 1.0 CD1 A:TYR159 4.8 26.7 1.0 CE1 A:TYR159 4.8 28.8 1.0 C A:GLU269 4.8 26.8 1.0 CA A:TYR296 4.9 25.0 1.0 N A:GLY270 4.9 25.5 1.0 O A:TYR296 4.9 26.0 1.0

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


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Blasnase-P55N within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:37.6 occ:0.00 O A:HOH702 2.4 38.9 1.0 O A:HOH678 2.6 47.8 1.0 O B:HOH673 3.0 41.6 1.0 OD2 A:ASP218 3.1 32.2 1.0 MG A:MG403 3.4 35.4 0.0 MG B:MG403 3.6 39.4 0.0 OE2 B:GLU207 3.7 38.5 1.0 O A:HOH555 3.7 40.7 1.0 O A:HOH605 4.1 27.2 1.0 CG A:ASP218 4.2 29.6 1.0 CD B:GLU207 4.4 38.2 1.0 O1 A:FMT405 4.4 35.1 0.0 CB A:ASP218 4.5 29.3 1.0 OE1 B:GLU207 4.7 43.0 1.0

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


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Blasnase-P55N within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:35.4 occ:0.00 O A:HOH702 2.2 38.9 1.0 O B:HOH673 3.3 41.6 1.0 O A:HOH557 3.3 33.5 1.0 MG A:MG402 3.4 37.6 0.0 O A:HOH569 4.0 27.3 1.0 O A:HOH703 4.3 41.7 1.0 O A:HOH687 4.6 43.2 1.0 OD1 A:ASP216 4.8 25.8 1.0 OD2 A:ASP216 4.9 26.6 1.0 O A:HOH605 4.9 27.2 1.0

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


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Blasnase-P55N within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg404 b:33.6 occ:0.00 O2 A:FMT405 2.1 32.5 0.0 O A:HOH679 2.2 43.0 1.0 O A:ASN246 2.3 28.3 1.0 O A:HOH688 2.3 40.0 1.0 OD2 A:ASP250 2.5 35.9 1.0 O A:HOH597 2.6 37.5 1.0 C A:FMT405 2.9 33.5 0.0 CG A:ASP250 3.5 34.1 1.0 C A:ASN246 3.5 30.4 1.0 OD1 A:ASP250 3.8 33.5 1.0 NH1 A:ARG223 3.8 30.0 1.0 O1 A:FMT405 4.1 35.1 0.0 N A:GLY219 4.1 25.2 1.0 CA A:ASN246 4.3 29.6 1.0 O A:HOH708 4.3 46.1 1.0 CA A:GLY219 4.4 28.2 1.0 O A:HOH590 4.4 30.5 1.0 N A:MET247 4.5 28.4 1.0 CB A:ASN246 4.5 28.6 1.0 CA A:MET247 4.6 26.8 1.0 CB A:ASP250 4.8 28.6 1.0 O A:HOH698 4.8 48.0 1.0 N A:ASP250 4.8 27.7 1.0 C A:MET247 5.0 29.1 1.0

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


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Blasnase-P55N within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg401 b:34.4 occ:0.00 OD2 B:ASP250 2.2 37.4 1.0 O B:ASN246 2.5 34.6 1.0 O B:HOH542 2.6 39.1 1.0 O1 B:FMT404 3.0 33.3 0.0 CG B:ASP250 3.1 36.2 1.0 C B:FMT404 3.4 33.6 0.0 OD1 B:ASP250 3.6 37.3 1.0 C B:ASN246 3.7 35.5 1.0 NH1 B:ARG223 4.0 32.4 1.0 O B:HOH580 4.2 38.3 1.0 N B:ASP250 4.2 33.2 1.0 CB B:ASP250 4.3 29.1 1.0 N B:GLY219 4.4 29.2 1.0 CA B:GLY219 4.5 31.3 1.0 O2 B:FMT404 4.5 33.7 0.0 CA B:ASN246 4.5 31.3 1.0 CA B:MET247 4.6 31.5 1.0 N B:MET247 4.6 31.0 1.0 C B:MET247 4.7 30.1 1.0 N B:GLY249 4.8 36.6 1.0 O B:MET247 4.8 32.5 1.0 CA B:ASP250 4.9 32.8 1.0 CB B:ASN246 4.9 32.9 1.0 CA B:GLY249 4.9 35.7 1.0 C B:GLY249 4.9 34.9 1.0

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


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Blasnase-P55N within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:31.2 occ:0.00 O B:HOH531 2.3 30.0 1.0 O B:HOH702 2.4 36.7 1.0 O B:ASP295 2.5 27.6 1.0 O B:HOH683 2.9 36.8 1.0 O B:GLU268 3.1 31.4 1.0 C B:ASP295 3.5 30.6 1.0 C B:GLU268 3.8 32.0 1.0 O B:HOH568 3.8 32.9 1.0 CB B:ASP295 4.0 30.8 1.0 O B:ALA267 4.0 29.5 1.0 CA B:ASP295 4.1 30.6 1.0 O B:HOH574 4.3 35.3 1.0 N B:GLU269 4.4 29.2 1.0 CA B:GLU269 4.4 27.5 1.0 N B:ASP297 4.4 26.4 1.0 O B:GLY270 4.5 33.3 1.0 C B:TYR296 4.6 30.6 1.0 CA B:GLU268 4.6 30.6 1.0 N B:TYR296 4.6 27.7 1.0 CG B:ASP295 4.7 33.1 1.0 CE1 B:TYR159 4.8 30.9 1.0 CD1 B:TYR159 4.8 29.8 1.0 C B:GLU269 4.9 31.0 1.0 CA B:TYR296 4.9 30.1 1.0 O B:TYR296 4.9 29.1 1.0 O B:HOH671 5.0 38.3 1.0 N B:GLY270 5.0 27.9 1.0

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


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of Blasnase-P55N within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg403 b:39.4 occ:0.00 O A:HOH555 2.6 40.7 1.0 O B:GLU228 2.6 40.2 1.0 OE1 B:GLU207 2.8 43.0 1.0 OE2 B:GLU207 2.9 38.5 1.0 CD B:GLU207 3.3 38.2 1.0 MG A:MG402 3.6 37.6 0.0 C B:GLU228 3.7 37.4 1.0 CB B:GLU228 3.8 35.8 1.0 O A:HOH678 4.0 47.8 1.0 CE A:LYS220 4.0 31.8 1.0 O B:HOH505 4.2 49.6 1.0 OD2 A:ASP218 4.2 32.2 1.0 NZ A:LYS220 4.3 32.0 1.0 CA B:GLU228 4.3 36.4 1.0 O B:HOH601 4.5 48.6 1.0 O B:HOH673 4.7 41.6 1.0 N B:GLY229 4.8 34.5 1.0 CG B:GLU207 4.8 33.0 1.0 OE2 B:GLU228 5.0 53.7 1.0 CG B:GLU228 5.0 37.1 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.