Magnesium in PDB 3reu: Crystal Structure of the Archaeal Asparagine Synthetase A Complexed with L-Aspartic Acid and Adenosine Triphosphate

The structure of Crystal Structure of the Archaeal Asparagine Synthetase A Complexed with L-Aspartic Acid and Adenosine Triphosphate, PDB code: 3reu was solved by M.Blaise, M.Frechin, C.Charron, H.Roy, C.Sauter, B.Lorber, V.Olieric, D.Kern, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	48.25 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	58.470, 61.180, 156.940, 90.00, 90.00, 90.00
R / Rfree (%)	17 / 21

The binding sites of Magnesium atom in the Crystal Structure of the Archaeal Asparagine Synthetase A Complexed with L-Aspartic Acid and Adenosine Triphosphate (pdb code 3reu). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 6 binding sites of Magnesium where determined in the Crystal Structure of the Archaeal Asparagine Synthetase A Complexed with L-Aspartic Acid and Adenosine Triphosphate, PDB code: 3reu:
Jump to Magnesium binding site number: 1; 2; 3; 4; 5; 6;

Magnesium binding site 1 out of 6 in the Crystal Structure of the Archaeal Asparagine Synthetase A Complexed with L-Aspartic Acid and Adenosine Triphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Crystal Structure of the Archaeal Asparagine Synthetase A Complexed with L-Aspartic Acid and Adenosine Triphosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg295 b:39.4 occ:1.00 O2A A:ATP298 2.4 50.4 0.4 O A:HOH441 2.5 25.0 1.0 O2B A:ATP298 2.5 37.4 0.7 O A:HOH473 2.6 45.1 1.0 OE1 A:GLU215 2.7 21.4 1.0 OG A:SER218 2.8 16.7 0.9 O3A A:ATP298 2.9 36.4 0.3 CB A:SER218 3.0 17.1 1.0 PA A:ATP298 3.1 42.7 1.0 PB A:ATP298 3.2 34.7 0.6 MG A:MG297 3.3 61.0 1.0 CD A:GLU215 3.5 27.0 1.0 OE2 A:GLU215 3.7 29.9 1.0 O A:HOH309 3.8 43.9 0.8 O5' A:ATP298 4.0 29.8 1.0 O3B A:ATP298 4.1 52.1 0.9 OD1 A:ASP206 4.1 16.3 1.0 NH1 A:ARG191 4.2 12.0 1.0 O A:HOH407 4.2 38.7 1.0 O1A A:ATP298 4.3 45.3 0.8 O1B A:ATP298 4.3 34.2 0.7 OD2 A:ASP206 4.4 19.6 1.0 CA A:SER218 4.5 10.9 1.0 O A:HOH445 4.5 39.8 1.0 CG A:ASP206 4.6 22.3 1.0 O3' A:ATP298 4.6 22.1 0.9 C3' A:ATP298 4.8 24.8 0.8 CG A:GLU215 4.9 19.9 1.0 CZ A:ARG191 4.9 21.3 1.0 OD2 A:ASP52 4.9 37.4 1.0 C5' A:ATP298 5.0 24.7 1.0

Magnesium binding site 2 out of 6 in the Crystal Structure of the Archaeal Asparagine Synthetase A Complexed with L-Aspartic Acid and Adenosine Triphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of the Archaeal Asparagine Synthetase A Complexed with L-Aspartic Acid and Adenosine Triphosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg296 b:53.7 occ:1.00 O1B A:ATP298 2.3 34.2 0.7 O A:HOH475 2.5 28.6 0.6 O2G A:ATP298 2.5 28.1 0.6 O A:HOH476 2.5 35.5 1.0 O A:HOH383 2.6 18.4 1.0 PG A:ATP298 3.1 26.6 0.4 O1G A:ATP298 3.1 22.2 0.5 PB A:ATP298 3.3 34.7 0.6 O A:ALA54 3.4 44.9 1.0 O3B A:ATP298 3.4 52.1 0.9 O2B A:ATP298 3.6 37.4 0.7 O A:HOH304 3.7 41.5 1.0 NH1 A:ARG99 4.2 15.7 1.0 C A:ALA54 4.2 45.6 1.0 OE2 A:GLU101 4.2 31.7 1.0 OE1 A:GLU101 4.4 46.0 1.0 NE2 A:HIS110 4.5 18.2 1.0 CB A:ALA54 4.5 44.6 1.0 O3G A:ATP298 4.5 33.8 1.0 O A:HOH309 4.5 43.9 0.8 O3A A:ATP298 4.6 36.4 0.3 MG A:MG297 4.7 61.0 1.0 CD A:GLU101 4.8 39.9 1.0 CA A:GLY55 4.8 37.9 1.0 CD2 A:HIS110 4.8 21.9 1.0 N7 A:ATP298 4.8 12.9 0.8 O A:HOH439 4.9 24.4 1.0 N A:GLY55 4.9 39.3 1.0

Magnesium binding site 3 out of 6 in the Crystal Structure of the Archaeal Asparagine Synthetase A Complexed with L-Aspartic Acid and Adenosine Triphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 3 of Crystal Structure of the Archaeal Asparagine Synthetase A Complexed with L-Aspartic Acid and Adenosine Triphosphate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg297 b:61.0 occ:1.00 OE2 A:GLU215 2.1 29.9 1.0 O1G A:ATP298 2.4 22.2 0.5 O2B A:ATP298 2.4 37.4 0.7 O A:HOH441 2.4 25.0 1.0 O3B A:ATP298 2.7 52.1 0.9 PG A:ATP298 2.9 26.6 0.4 CD A:GLU215 3.0 27.0 1.0 PB A:ATP298 3.0 34.7 0.6 CB A:ALA54 3.2 44.6 1.0 OE1 A:GLU215 3.2 21.4 1.0 MG A:MG295 3.3 39.4 1.0 O3G A:ATP298 3.4 33.8 1.0 O3A A:ATP298 4.0 36.4 0.3 O1B A:ATP298 4.2 34.2 0.7 O2G A:ATP298 4.2 28.1 0.6 CG A:GLU215 4.4 19.9 1.0 O A:HOH407 4.4 38.7 1.0 OD2 A:ASP206 4.5 19.6 1.0 CB A:GLU215 4.6 17.3 1.0 CA A:ALA54 4.6 43.4 1.0 MG A:MG296 4.7 53.7 1.0 O A:HOH473 4.9 45.1 1.0

Magnesium binding site 4 out of 6 in the Crystal Structure of the Archaeal Asparagine Synthetase A Complexed with L-Aspartic Acid and Adenosine Triphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 4 of Crystal Structure of the Archaeal Asparagine Synthetase A Complexed with L-Aspartic Acid and Adenosine Triphosphate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg296 b:28.8 occ:1.00 O2A B:ATP299 2.1 37.9 0.4 O2B B:ATP299 2.2 22.2 0.8 OG B:SER218 2.3 17.8 1.0 OE2 B:GLU215 2.3 24.4 1.0 O B:HOH354 2.3 21.9 1.0 O B:HOH371 2.4 40.2 1.0 O3A B:ATP299 3.0 0.8 0.0 PA B:ATP299 3.0 33.3 1.0 MG B:MG297 3.0 45.5 1.0 PB B:ATP299 3.1 27.5 0.5 CB B:SER218 3.2 11.5 1.0 CD B:GLU215 3.2 27.8 1.0 OE1 B:GLU215 3.5 36.6 1.0 O B:HOH386 3.9 43.2 1.0 O3B B:ATP299 4.0 28.0 0.8 O1A B:ATP299 4.0 21.0 1.0 O5' B:ATP299 4.0 31.6 1.0 O1B B:ATP299 4.1 27.9 0.6 OD2 B:ASP206 4.2 25.5 1.0 OD1 B:ASP206 4.2 23.4 1.0 O B:HOH359 4.2 33.7 1.0 O3' B:ATP299 4.3 22.4 1.0 OD2 B:ASP295 4.3 46.2 0.7 NH1 B:ARG191 4.4 22.5 1.0 CA B:SER218 4.5 16.2 1.0 CG B:ASP206 4.5 24.9 1.0 CG B:GLU215 4.6 21.5 1.0 C3' B:ATP299 4.6 18.2 1.0 O B:HOH385 4.7 51.4 1.0 O B:HOH334 4.7 23.0 1.0 O1G B:ATP299 4.8 25.3 0.5 N B:SER218 4.9 21.6 1.0 OD2 B:ASP52 4.9 57.3 1.0 PG B:ATP299 5.0 23.8 0.5

Magnesium binding site 5 out of 6 in the Crystal Structure of the Archaeal Asparagine Synthetase A Complexed with L-Aspartic Acid and Adenosine Triphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 5 of Crystal Structure of the Archaeal Asparagine Synthetase A Complexed with L-Aspartic Acid and Adenosine Triphosphate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg297 b:45.5 occ:1.00 O2B B:ATP299 2.2 22.2 0.8 O B:HOH354 2.3 21.9 1.0 O B:HOH385 2.3 51.4 1.0 O1G B:ATP299 2.4 25.3 0.5 OE1 B:GLU215 2.4 36.6 1.0 MG B:MG296 3.0 28.8 1.0 PB B:ATP299 3.3 27.5 0.5 CD B:GLU215 3.3 27.8 1.0 PG B:ATP299 3.3 23.8 0.5 O3B B:ATP299 3.4 28.0 0.8 OE2 B:GLU215 3.5 24.4 1.0 O B:HOH359 3.6 33.7 1.0 O1B B:ATP299 4.1 27.9 0.6 O B:HOH371 4.2 40.2 1.0 OD2 B:ASP206 4.2 25.5 1.0 O3G B:ATP299 4.3 22.9 0.8 O3A B:ATP299 4.3 0.8 0.0 O2G B:ATP299 4.4 23.3 0.7 O B:HOH410 4.4 43.3 1.0 O B:HOH409 4.6 31.9 1.0 OD1 B:ASP52 4.7 60.3 1.0 CG B:GLU215 4.7 21.5 1.0 OG B:SER218 4.7 17.8 1.0 O B:HOH395 4.8 49.4 1.0 O2A B:ATP299 4.8 37.9 0.4 OD2 B:ASP52 4.8 57.3 1.0 O B:HOH386 4.9 43.2 1.0 MG B:MG298 5.0 64.5 1.0

Magnesium binding site 6 out of 6 in the Crystal Structure of the Archaeal Asparagine Synthetase A Complexed with L-Aspartic Acid and Adenosine Triphosphate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 6 of Crystal Structure of the Archaeal Asparagine Synthetase A Complexed with L-Aspartic Acid and Adenosine Triphosphate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg298 b:64.5 occ:1.00 O1B B:ATP299 2.3 27.9 0.6 O2G B:ATP299 2.3 23.3 0.7 O B:HOH381 2.4 26.7 1.0 O B:HOH308 2.5 57.8 1.0 O B:HOH387 2.6 51.4 1.0 O B:HOH395 2.9 49.4 1.0 PG B:ATP299 3.2 23.8 0.5 PB B:ATP299 3.3 27.5 0.5 O3B B:ATP299 3.3 28.0 0.8 O1G B:ATP299 3.8 25.3 0.5 O2B B:ATP299 3.9 22.2 0.8 OE1 B:GLU101 4.2 38.7 1.0 OE2 B:GLU101 4.2 30.7 1.0 NH1 B:ARG99 4.2 18.2 1.0 NE2 B:HIS110 4.3 24.4 1.0 O3G B:ATP299 4.5 22.9 0.8 N7 B:ATP299 4.5 17.9 0.9 O3A B:ATP299 4.5 0.8 0.0 O B:HOH385 4.6 51.4 1.0 CD2 B:HIS110 4.6 21.1 1.0 CD B:GLU101 4.7 37.3 1.0 MG B:MG297 5.0 45.5 1.0

M.Blaise, M.Frechin, V.Olieric, C.Charron, C.Sauter, B.Lorber, H.Roy, D.Kern. Crystal Structure of the Archaeal Asparagine Synthetase: Interrelation with Aspartyl-Trna and Asparaginyl-Trna Synthetases. J.Mol.Biol. V. 412 437 2011.
ISSN: ISSN 0022-2836
PubMed: 21820443
DOI: 10.1016/J.JMB.2011.07.050