Magnesium in PDB 8h4e: Blasnase-T13A/P55N with D-Asn

The structure of Blasnase-T13A/P55N with D-Asn, PDB code: 8h4e 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)	19.97 / 2.06
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	92.42, 92.42, 232.452, 90, 90, 90
R / Rfree (%)	19.6 / 22.1

The binding sites of Magnesium atom in the Blasnase-T13A/P55N with D-Asn (pdb code 8h4e). 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/P55N with D-Asn, PDB code: 8h4e:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Blasnase-T13A/P55N with D-Asn


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 with D-Asn within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:42.1 occ:0.00 OD2 A:ASP250 2.4 45.3 1.0 O A:ASN246 2.5 40.6 1.0 O A:HOH557 2.5 42.4 1.0 O2 A:FMT403 2.6 40.4 0.0 CG A:ASP250 3.4 43.8 1.0 C A:FMT403 3.4 40.6 0.0 C A:ASN246 3.7 44.2 1.0 OD1 A:ASP250 3.7 42.2 1.0 NH1 A:ARG223 3.7 40.7 1.0 N A:GLY219 4.3 36.6 1.0 O A:HOH584 4.4 43.6 1.0 CA A:GLY219 4.5 35.0 1.0 CA A:ASN246 4.5 39.1 1.0 O1 A:FMT403 4.6 41.6 0.0 N A:MET247 4.6 37.2 1.0 CB A:ASN246 4.6 39.6 1.0 CA A:MET247 4.7 37.8 1.0 N A:ASP250 4.7 37.1 1.0 CB A:ASP250 4.7 36.2 1.0 CZ A:ARG223 5.0 45.5 1.0

Magnesium binding site 2 out of 4 in the Blasnase-T13A/P55N with D-Asn


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 with D-Asn within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:37.1 occ:0.00 O A:ASP295 2.6 35.1 1.0 O A:HOH576 2.7 38.5 1.0 O A:HOH547 3.0 36.2 1.0 O A:HOH603 3.0 44.0 1.0 O A:GLU268 3.3 43.1 1.0 N A:ASP297 3.6 31.4 1.0 C A:ASP295 3.7 33.9 1.0 O A:ALA267 4.0 33.0 1.0 C A:GLU268 4.0 38.0 1.0 C A:TYR296 4.0 36.2 1.0 CA A:ASP297 4.2 33.3 1.0 CB A:ASP297 4.4 34.6 1.0 CA A:GLU268 4.4 37.4 1.0 O A:TYR296 4.5 35.0 1.0 N A:TYR296 4.5 35.6 1.0 CA A:TYR296 4.5 35.1 1.0 O A:HOH541 4.5 38.7 1.0 CA A:ASP295 4.6 35.4 1.0 CB A:ASP295 4.7 34.4 1.0 CD1 A:TYR159 4.8 35.7 1.0 N A:GLU269 4.9 38.0 1.0 CE1 A:TYR159 5.0 37.6 1.0 C A:ALA267 5.0 33.1 1.0

Magnesium binding site 3 out of 4 in the Blasnase-T13A/P55N with D-Asn


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 with D-Asn within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg401 b:47.2 occ:0.00 OE2 B:GLU207 2.8 48.8 1.0 OE1 B:GLU207 2.9 56.3 1.0 CD B:GLU207 3.2 47.7 1.0 O B:GLU228 3.3 48.7 1.0 OD2 A:ASP218 3.5 42.3 1.0 CE A:LYS220 3.8 39.5 1.0 O A:HOH626 3.8 67.7 1.0 CB B:GLU228 3.9 45.0 1.0 NZ A:LYS220 4.0 41.3 1.0 O B:HOH510 4.2 62.2 1.0 C B:GLU228 4.3 42.0 1.0 O1 B:FMT405 4.5 42.3 0.0 O1 A:FMT403 4.6 41.6 0.0 CA B:GLU228 4.7 43.5 1.0 CG B:GLU207 4.7 43.5 1.0 CG A:ASP218 4.7 37.9 1.0 OE2 B:GLU228 4.8 56.0 1.0 CG B:GLU228 5.0 46.2 1.0

Magnesium binding site 4 out of 4 in the Blasnase-T13A/P55N with D-Asn


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 with D-Asn within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:42.3 occ:0.00 O B:ASP295 2.6 39.3 1.0 O B:HOH621 2.7 40.9 1.0 O B:GLU268 2.9 41.4 1.0 C B:GLU268 3.5 43.5 1.0 C B:ASP295 3.6 41.7 1.0 O B:ALA267 3.7 38.9 1.0 O B:HOH592 3.8 42.8 1.0 CB B:ASP295 4.0 42.6 1.0 CA B:ASP295 4.1 44.5 1.0 CA B:GLU268 4.2 42.0 1.0 N B:GLU269 4.3 40.4 1.0 O B:GLY270 4.4 45.3 1.0 N B:ASP297 4.5 34.9 1.0 CA B:GLU269 4.5 42.0 1.0 O B:HOH598 4.5 49.7 1.0 C B:TYR296 4.6 40.1 1.0 O B:HOH654 4.6 64.3 1.0 C B:ALA267 4.6 39.9 1.0 N B:TYR296 4.7 39.3 1.0 O B:HOH584 4.7 52.1 1.0 CG B:ASP295 4.8 44.8 1.0 C B:GLU269 4.9 43.6 1.0 O B:TYR296 4.9 38.0 1.0 N B:GLU268 4.9 40.0 1.0 N B:GLY270 4.9 40.6 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.