Magnesium in PDB 8h49: Blasnase-M57P

The structure of Blasnase-M57P, PDB code: 8h49 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)	41.39 / 2.00
Space group	P 41 21 2
Cell size a, b, c (Å), α, β, γ (°)	91.674, 91.674, 231.918, 90, 90, 90
R / Rfree (%)	19.1 / 21.4

The binding sites of Magnesium atom in the Blasnase-M57P (pdb code 8h49). 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-M57P, PDB code: 8h49:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6; 7;

Magnesium binding site 1 out of 7 in the Blasnase-M57P


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Blasnase-M57P within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:36.7 occ:0.00 O A:ASP295 2.2 38.4 1.0 O A:HOH559 2.4 35.5 1.0 O A:HOH637 3.0 41.6 1.0 O A:GLU268 3.1 38.1 1.0 C A:ASP295 3.2 38.4 1.0 C A:GLU268 3.9 37.5 1.0 CB A:ASP295 3.9 35.1 1.0 CA A:ASP295 4.0 34.6 1.0 O A:HOH582 4.0 42.2 1.0 N A:ASP297 4.0 31.5 1.0 C A:TYR296 4.2 36.8 1.0 O A:ALA267 4.2 34.7 1.0 N A:TYR296 4.3 35.6 1.0 O A:HOH542 4.4 42.6 1.0 CA A:TYR296 4.5 33.5 1.0 O A:HOH624 4.5 45.0 1.0 CA A:GLU269 4.5 32.8 1.0 N A:GLU269 4.5 33.9 1.0 O A:GLY270 4.6 36.0 1.0 O A:TYR296 4.7 38.1 1.0 CG A:ASP295 4.7 40.4 1.0 CA A:ASP297 4.8 30.8 1.0 CA A:GLU268 4.8 35.5 1.0 CD1 A:TYR159 4.8 37.8 1.0 CE1 A:TYR159 4.9 36.1 1.0 C A:GLU269 5.0 34.7 1.0

Magnesium binding site 2 out of 7 in the Blasnase-M57P


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Blasnase-M57P within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg402 b:45.9 occ:0.00 MG B:MG403 2.3 46.0 0.0 O B:HOH684 2.6 58.6 1.0 O A:HOH636 3.5 44.4 1.0 O A:HOH587 3.9 40.4 1.0 O A:HOH564 4.0 38.8 1.0 O1 B:FMT406 4.2 41.0 0.0 O A:HOH560 4.2 43.6 1.0 O B:HOH602 4.7 43.0 1.0 O A:HOH642 4.7 47.6 1.0 C B:FMT406 4.8 40.7 0.0 CD B:GLU207 4.8 49.2 1.0 OD2 A:ASP218 4.9 41.7 1.0 OE1 B:GLU207 4.9 54.8 1.0 OE2 B:GLU207 4.9 50.4 1.0 OD1 A:ASP216 5.0 37.0 1.0 OD2 A:ASP216 5.0 36.1 1.0

Magnesium binding site 3 out of 7 in the Blasnase-M57P


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Blasnase-M57P within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg403 b:41.6 occ:0.00 O1 A:FMT404 2.1 41.2 0.0 O A:HOH594 2.2 43.6 1.0 OD2 A:ASP250 2.4 43.3 1.0 O A:ASN246 2.8 41.4 1.0 C A:FMT404 2.8 41.4 0.0 CG A:ASP250 3.3 42.1 1.0 NH1 A:ARG223 3.5 40.3 1.0 OD1 A:ASP250 3.6 44.7 1.0 C A:ASN246 3.9 45.0 1.0 O2 A:FMT404 4.0 41.5 0.0 N A:GLY219 4.4 39.7 1.0 CA A:GLY219 4.5 39.7 1.0 O A:HOH552 4.5 42.2 1.0 CA A:ASN246 4.6 43.5 1.0 CB A:ASP250 4.6 38.8 1.0 CB A:ASN246 4.6 34.0 1.0 N A:ASP250 4.7 38.3 1.0 CZ A:ARG223 4.8 46.4 1.0 N A:MET247 5.0 37.9 1.0

Magnesium binding site 4 out of 7 in the Blasnase-M57P


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Blasnase-M57P within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg401 b:46.6 occ:0.00 O1 B:FMT405 2.1 45.6 0.0 O B:HOH613 2.4 52.0 1.0 OD2 B:ASP250 2.7 48.5 1.0 O B:ASN246 2.7 45.8 1.0 C B:FMT405 2.9 45.7 0.0 CG B:ASP250 3.7 48.2 1.0 C B:ASN246 3.9 46.1 1.0 OD1 B:ASP250 3.9 51.8 1.0 O2 B:FMT405 4.0 45.4 0.0 NH1 B:ARG223 4.1 45.8 1.0 CA B:ASN246 4.5 41.3 1.0 O B:HOH548 4.5 48.5 1.0 CB B:ASN246 4.6 47.7 1.0 N B:GLY219 4.7 43.1 1.0 N B:ASP250 4.8 43.5 1.0 CA B:GLY219 4.9 39.3 1.0 O B:HOH666 4.9 57.1 1.0 N B:MET247 4.9 41.1 1.0 CB B:ASP250 5.0 42.8 1.0

Magnesium binding site 5 out of 7 in the Blasnase-M57P


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Blasnase-M57P within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg402 b:39.1 occ:0.00 O B:HOH654 2.4 45.5 1.0 O B:HOH586 2.4 38.8 1.0 O B:ASP295 2.5 37.6 1.0 O B:GLU268 2.9 38.1 1.0 C B:ASP295 3.6 42.1 1.0 O B:HOH598 3.6 44.2 1.0 C B:GLU268 3.7 38.8 1.0 O B:HOH568 4.1 39.0 1.0 CB B:ASP295 4.1 38.4 1.0 O B:ALA267 4.1 34.7 1.0 N B:ASP297 4.2 36.1 1.0 CA B:ASP295 4.2 42.7 1.0 N B:GLU269 4.4 33.6 1.0 C B:TYR296 4.5 40.7 1.0 CA B:GLU269 4.5 39.1 1.0 CD1 B:TYR159 4.6 38.7 1.0 N B:TYR296 4.6 37.6 1.0 CA B:GLU268 4.6 35.9 1.0 CE1 B:TYR159 4.7 37.2 1.0 CA B:TYR296 4.8 36.5 1.0 CG B:ASP295 4.8 46.0 1.0 O B:GLY270 4.9 39.8 1.0 O B:HOH567 4.9 48.2 1.0 O B:TYR296 4.9 38.1 1.0 CA B:ASP297 4.9 37.3 1.0 C B:GLU269 5.0 39.8 1.0

Magnesium binding site 6 out of 7 in the Blasnase-M57P


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Blasnase-M57P within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg403 b:46.0 occ:0.00 O A:HOH636 2.2 44.4 1.0 MG A:MG402 2.3 45.9 0.0 OE2 B:GLU207 2.7 50.4 1.0 O A:HOH587 2.9 40.4 1.0 CD B:GLU207 3.0 49.2 1.0 OD2 A:ASP218 3.1 41.7 1.0 OE1 B:GLU207 3.3 54.8 1.0 O B:HOH684 3.4 58.6 1.0 MG B:MG404 3.5 48.5 0.0 CG B:GLU207 3.8 47.0 1.0 CG A:ASP218 4.1 40.7 1.0 NZ A:LYS220 4.5 42.4 1.0 O1 B:FMT406 4.5 41.0 0.0 CB A:ASP218 4.7 41.0 1.0 CB B:GLU207 4.7 46.0 1.0 C B:FMT406 4.7 40.7 0.0 O A:HOH564 4.7 38.8 1.0 O B:HOH562 4.7 44.5 1.0

Magnesium binding site 7 out of 7 in the Blasnase-M57P


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 7 of Blasnase-M57P within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg404 b:48.5 occ:0.00 O A:HOH636 2.3 44.4 1.0 OE2 B:GLU207 2.6 50.4 1.0 O B:GLU228 2.7 54.0 1.0 OE1 B:GLU207 2.8 54.8 1.0 CD B:GLU207 3.1 49.2 1.0 MG B:MG403 3.5 46.0 0.0 C B:GLU228 3.8 47.0 1.0 OD2 A:ASP218 3.8 41.7 1.0 CE A:LYS220 3.9 41.0 1.0 CB B:GLU228 3.9 44.5 1.0 NZ A:LYS220 4.0 42.4 1.0 CA B:GLU228 4.4 45.8 1.0 OE1 B:GLU228 4.4 65.1 1.0 CG B:GLU207 4.6 47.0 1.0 N B:GLY229 4.8 42.8 1.0 O B:HOH684 4.9 58.6 1.0 CG A:ASP218 4.9 40.7 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.