Magnesium in PDB 8h4f: Blasnase-T13A/P55F with D-Asn

The structure of Blasnase-T13A/P55F with D-Asn, PDB code: 8h4f 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)	19.82 / 1.90
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	92.443, 92.443, 231.509, 90, 90, 90
R / Rfree (%)	19.1 / 21.1

The binding sites of Magnesium atom in the Blasnase-T13A/P55F with D-Asn (pdb code 8h4f). 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 with D-Asn, PDB code: 8h4f:
Jump to Magnesium binding site number: 1; 2; 3; 4;

Magnesium binding site 1 out of 4 in the Blasnase-T13A/P55F 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/P55F with D-Asn within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:40.5 occ:0.00 OE2 B:GLU207 2.3 39.9 1.0 O A:HOH504 2.4 42.2 1.0 O B:HOH715 2.4 45.8 1.0 O A:HOH583 2.5 31.5 1.0 O A:HOH502 2.5 40.9 1.0 OD2 A:ASP218 2.5 40.5 1.0 O1 A:FMT404 3.1 40.1 0.0 CD B:GLU207 3.2 44.5 1.0 CG A:ASP218 3.4 37.3 1.0 MG B:MG401 3.6 44.8 0.0 O A:HOH607 3.8 50.4 1.0 OE1 B:GLU207 3.9 46.4 1.0 CB A:ASP218 3.9 34.4 1.0 CG B:GLU207 4.0 39.4 1.0 NZ A:LYS220 4.1 37.4 1.0 C A:FMT404 4.2 40.8 0.0 O B:HOH580 4.3 38.0 1.0 OD1 A:ASP218 4.4 35.0 1.0 O A:HOH571 4.5 32.5 1.0 O1 B:FMT403 4.5 36.4 0.0 O A:HOH670 4.6 53.7 1.0 O A:HOH516 4.8 36.9 1.0 C B:FMT403 4.9 35.2 0.0 O2 A:FMT404 4.9 40.9 0.0 CB B:GLU207 4.9 39.4 1.0

Magnesium binding site 2 out of 4 in the Blasnase-T13A/P55F 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/P55F with D-Asn within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:39.4 occ:0.00 O2 A:FMT403 2.2 40.1 0.0 O A:HOH678 2.3 49.5 1.0 O A:ASN246 2.4 35.6 1.0 O A:HOH558 2.5 40.0 1.0 OD2 A:ASP250 2.5 41.6 1.0 C A:FMT403 3.1 41.5 0.0 CG A:ASP250 3.5 38.6 1.0 C A:ASN246 3.6 39.5 1.0 OD1 A:ASP250 3.9 39.3 1.0 NH1 A:ARG223 3.9 36.1 1.0 O1 A:FMT403 4.2 42.8 0.0 O A:HOH602 4.2 35.3 1.0 CA A:ASN246 4.3 35.8 1.0 N A:GLY219 4.3 32.8 1.0 O A:HOH646 4.4 56.5 1.0 CB A:ASN246 4.5 34.1 1.0 N A:MET247 4.5 33.0 1.0 CA A:GLY219 4.5 35.0 1.0 CA A:MET247 4.7 33.1 1.0 O A:HOH695 4.7 48.8 1.0 N A:ASP250 4.7 32.9 1.0 CB A:ASP250 4.8 33.2 1.0 C A:MET247 5.0 33.8 1.0

Magnesium binding site 3 out of 4 in the Blasnase-T13A/P55F 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/P55F with D-Asn within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg401 b:44.8 occ:0.00 O A:HOH607 2.0 50.4 1.0 O B:HOH715 2.5 45.8 1.0 OE1 B:GLU207 2.6 46.4 1.0 OE2 B:GLU207 2.7 39.9 1.0 O B:GLU228 2.8 46.9 1.0 CD B:GLU207 3.0 44.5 1.0 MG A:MG401 3.6 40.5 0.0 C B:GLU228 3.8 43.1 1.0 CB B:GLU228 3.9 40.6 1.0 OD2 A:ASP218 4.0 40.5 1.0 O A:HOH670 4.0 53.7 1.0 CE A:LYS220 4.1 33.7 1.0 NZ A:LYS220 4.3 37.4 1.0 O B:HOH573 4.4 55.8 1.0 O A:HOH504 4.4 42.2 1.0 CA B:GLU228 4.4 40.6 1.0 CG B:GLU207 4.6 39.4 1.0 N B:GLY229 4.8 39.1 1.0

Magnesium binding site 4 out of 4 in the Blasnase-T13A/P55F 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/P55F with D-Asn within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:35.2 occ:0.00 O B:HOH558 2.3 37.3 1.0 O B:ASP295 2.5 32.5 1.0 O B:HOH700 2.5 42.7 1.0 O B:HOH654 2.9 43.1 1.0 O B:GLU268 3.0 33.2 1.0 C B:ASP295 3.6 33.6 1.0 O B:HOH556 3.7 38.2 1.0 C B:GLU268 3.8 33.3 1.0 O B:ALA267 4.0 32.3 1.0 CB B:ASP295 4.0 32.8 1.0 CA B:ASP295 4.1 34.8 1.0 O B:HOH587 4.2 40.4 1.0 O B:HOH549 4.3 39.7 1.0 N B:ASP297 4.3 29.8 1.0 O B:HOH626 4.4 30.0 1.0 N B:GLU269 4.4 32.9 1.0 CA B:GLU269 4.4 32.1 1.0 C B:TYR296 4.5 34.2 1.0 O B:GLY270 4.6 34.3 1.0 CA B:GLU268 4.6 33.8 1.0 N B:TYR296 4.6 30.5 1.0 CG B:ASP295 4.8 38.0 1.0 O B:TYR296 4.8 35.0 1.0 CD1 B:TYR159 4.8 34.6 1.0 CE1 B:TYR159 4.9 32.1 1.0 CA B:TYR296 4.9 33.4 1.0 C B:GLU269 4.9 34.5 1.0 CA B:ASP297 5.0 28.3 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.