Magnesium in PDB 2xgt: Asparaginyl-Trna Synthetase From Brugia Malayi Complexed with the Sulphamoyl Analogue of Asparaginyl-Adenylate

All present enzymatic activity of Asparaginyl-Trna Synthetase From Brugia Malayi Complexed with the Sulphamoyl Analogue of Asparaginyl-Adenylate:
6.1.1.4;

The structure of Asparaginyl-Trna Synthetase From Brugia Malayi Complexed with the Sulphamoyl Analogue of Asparaginyl-Adenylate, PDB code: 2xgt was solved by T.Crepin, M.Haertlein, M.Kron, S.Cusack, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	94.92 / 1.90
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.510, 125.700, 144.268, 90.00, 90.00, 90.00
R / Rfree (%)	20.231 / 25.017

The binding sites of Magnesium atom in the Asparaginyl-Trna Synthetase From Brugia Malayi Complexed with the Sulphamoyl Analogue of Asparaginyl-Adenylate (pdb code 2xgt). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Asparaginyl-Trna Synthetase From Brugia Malayi Complexed with the Sulphamoyl Analogue of Asparaginyl-Adenylate, PDB code: 2xgt:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Asparaginyl-Trna Synthetase From Brugia Malayi Complexed with the Sulphamoyl Analogue of Asparaginyl-Adenylate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Asparaginyl-Trna Synthetase From Brugia Malayi Complexed with the Sulphamoyl Analogue of Asparaginyl-Adenylate within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg1551 b:15.3 occ:1.00 OAY A:NSS1550 2.3 9.2 1.0 O A:HOH2287 2.4 16.7 1.0 OE2 A:GLU471 2.5 13.6 1.0 O A:HOH2244 2.5 19.1 1.0 O A:HOH2243 2.6 12.6 1.0 O A:HOH2247 2.6 31.0 1.0 CD A:GLU471 3.2 13.8 1.0 OE1 A:GLU471 3.2 17.8 1.0 O A:HOH2246 3.6 29.2 1.0 SBE A:NSS1550 3.6 10.2 1.0 O A:HOH2226 4.0 23.0 1.0 OAX A:NSS1550 4.1 9.1 1.0 O A:HOH2286 4.2 7.9 1.0 O A:HOH2118 4.3 13.5 1.0 OD1 A:ASP463 4.4 14.6 1.0 OD2 A:ASP463 4.4 16.9 1.0 O A:HOH2245 4.4 36.5 1.0 O3' A:NSS1550 4.5 8.1 1.0 NAT A:NSS1550 4.5 8.0 1.0 CA A:GLY474 4.5 10.7 1.0 C3' A:NSS1550 4.5 10.7 1.0 O5' A:NSS1550 4.6 10.4 1.0 CG A:GLU471 4.6 12.8 1.0 CG A:ASP463 4.7 14.1 1.0 NZ A:LYS445 4.8 16.4 1.0

Magnesium binding site 2 out of 2 in the Asparaginyl-Trna Synthetase From Brugia Malayi Complexed with the Sulphamoyl Analogue of Asparaginyl-Adenylate


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Asparaginyl-Trna Synthetase From Brugia Malayi Complexed with the Sulphamoyl Analogue of Asparaginyl-Adenylate within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg1551 b:26.3 occ:1.00 O B:HOH2208 2.3 13.4 1.0 OAX B:NSS1550 2.4 14.5 1.0 O B:HOH2173 2.4 18.5 1.0 OE2 B:GLU471 2.5 16.5 1.0 O B:HOH2175 2.5 24.0 1.0 CD B:GLU471 3.3 21.3 1.0 OE1 B:GLU471 3.4 23.6 1.0 SBE B:NSS1550 3.7 15.3 1.0 O B:HOH2176 3.9 23.3 1.0 OAY B:NSS1550 4.1 15.2 1.0 O B:HOH2205 4.1 19.7 1.0 OD1 B:ASP463 4.3 21.9 1.0 O B:HOH2094 4.3 17.1 1.0 OD2 B:ASP463 4.3 24.2 1.0 NAT B:NSS1550 4.6 13.7 1.0 CG B:ASP463 4.6 20.7 1.0 O3' B:NSS1550 4.6 16.0 1.0 O5' B:NSS1550 4.7 15.5 1.0 CG B:GLU471 4.7 19.8 1.0 CA B:GLY474 4.7 15.2 1.0 C3' B:NSS1550 4.8 14.7 1.0 NZ B:LYS445 4.8 20.9 1.0

T.Crepin, F.Peterson, M.Haertlein, D.Jensen, C.Wang, S.Cusack, M.Kron. A Hybrid Structural Model of the Complete Brugia Malayi Cytoplasmic Asparaginyl-Trna Synthetase. J.Mol.Biol. V. 405 1056 2011.
ISSN: ISSN 0022-2836
PubMed: 21134380
DOI: 10.1016/J.JMB.2010.11.049