Magnesium in PDB 5e3i: Crystal Structure of A Histidyl-Trna Synthetase From Acinetobacter Baumannii with Bound L-Histidine and Atp

All present enzymatic activity of Crystal Structure of A Histidyl-Trna Synthetase From Acinetobacter Baumannii with Bound L-Histidine and Atp:
6.1.1.21;

The structure of Crystal Structure of A Histidyl-Trna Synthetase From Acinetobacter Baumannii with Bound L-Histidine and Atp, PDB code: 5e3i was solved by Seattle Structural Genomics Center For Infectious Disease, Seattlestructural Genomics Center For Infectious Disease (Ssgcid), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	47.54 / 2.20
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	88.810, 103.070, 246.300, 90.00, 90.00, 90.00
R / Rfree (%)	16.5 / 20.5

The binding sites of Magnesium atom in the Crystal Structure of A Histidyl-Trna Synthetase From Acinetobacter Baumannii with Bound L-Histidine and Atp (pdb code 5e3i). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of A Histidyl-Trna Synthetase From Acinetobacter Baumannii with Bound L-Histidine and Atp, PDB code: 5e3i:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of A Histidyl-Trna Synthetase From Acinetobacter Baumannii with Bound L-Histidine and Atp


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 A Histidyl-Trna Synthetase From Acinetobacter Baumannii with Bound L-Histidine and Atp within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg500 b:44.8 occ:1.00 O2B A:ATP501 2.0 36.1 0.9 O A:HOH731 2.0 46.6 1.0 O A:HOH639 2.0 38.2 1.0 O3G A:ATP501 2.1 42.7 0.9 O A:HOH627 2.1 39.7 1.0 O A:HOH663 2.3 39.6 1.0 PB A:ATP501 3.3 42.0 0.9 PG A:ATP501 3.4 41.3 0.9 O3B A:ATP501 3.7 41.0 0.9 O A:HOH820 3.9 49.8 1.0 NH1 A:ARG115 3.9 28.9 1.0 NH1 A:ARG123 4.0 43.0 1.0 O1G A:ATP501 4.1 47.4 0.9 O1B A:ATP501 4.2 42.2 0.9 OE1 A:GLU66 4.2 41.1 1.0 OE2 A:GLU66 4.2 54.9 1.0 OE1 A:GLU117 4.3 50.1 1.0 OE2 A:GLU117 4.3 39.6 1.0 O3A A:ATP501 4.4 50.6 0.9 O2G A:ATP501 4.6 41.9 0.9 CD A:GLU66 4.7 48.5 1.0 CD A:GLU117 4.7 47.0 1.0 N7 A:ATP501 4.7 24.6 0.9 O A:HOH718 4.8 57.4 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of A Histidyl-Trna Synthetase From Acinetobacter Baumannii with Bound L-Histidine and Atp


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 A Histidyl-Trna Synthetase From Acinetobacter Baumannii with Bound L-Histidine and Atp within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg500 b:38.2 occ:1.00 O B:HOH634 1.9 38.2 1.0 O1B B:ATP501 2.1 35.0 0.9 O3G B:ATP501 2.1 31.6 0.9 O B:HOH643 2.1 28.3 1.0 O B:HOH608 2.2 31.5 1.0 O B:HOH698 2.2 39.6 1.0 PB B:ATP501 3.4 38.1 0.9 PG B:ATP501 3.4 39.8 0.9 O3B B:ATP501 3.6 36.8 0.9 NH1 B:ARG115 3.8 31.5 1.0 NH1 B:ARG123 3.9 46.4 1.0 OE2 B:GLU117 4.1 40.2 1.0 O2G B:ATP501 4.2 42.0 0.9 OE1 B:GLU66 4.2 37.0 1.0 OE1 B:GLU117 4.3 37.3 1.0 OE2 B:GLU66 4.3 43.7 1.0 O3A B:ATP501 4.3 49.0 0.9 O2B B:ATP501 4.4 38.5 0.9 N7 B:ATP501 4.5 24.0 0.9 O1G B:ATP501 4.6 35.5 0.9 CD B:GLU117 4.6 41.2 1.0 CD B:GLU66 4.7 39.6 1.0 C8 B:ATP501 4.9 24.8 0.9

Ssgcid, C.M.Lukacs, D.M.Dranow, D.Lorimer, T.E.Edwards. Crystal Structure of A Histidyl-Trna Synthetase From Acinetobacter Baumannii with Bound L-Histidine and Atp To Be Published.