Magnesium in PDB 1m74: Crystal Structure of Mg-Adp-Bound Seca From Bacillus Subtilis

The structure of Crystal Structure of Mg-Adp-Bound Seca From Bacillus Subtilis, PDB code: 1m74 was solved by J.F.Hunt, S.Weinkauf, L.Henry, J.J.Fak, P.Mcnicholas, D.B.Oliver, J.Deisenhofer, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	49.45 / 3.00
Space group	P 31 1 2
Cell size a, b, c (Å), α, β, γ (°)	131.245, 131.245, 150.453, 90.00, 90.00, 120.00
R / Rfree (%)	21.7 / 29.1

The binding sites of Magnesium atom in the Crystal Structure of Mg-Adp-Bound Seca From Bacillus Subtilis (pdb code 1m74). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total only one binding site of Magnesium was determined in the Crystal Structure of Mg-Adp-Bound Seca From Bacillus Subtilis, PDB code: 1m74:

Magnesium binding site 1 out of 1 in the Crystal Structure of Mg-Adp-Bound Seca From Bacillus Subtilis


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 Mg-Adp-Bound Seca From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg902 b:86.1 occ:1.00 O A:HOH1146 1.4 0.1 1.0 O A:HOH1147 1.4 95.8 1.0 O1B A:ADP901 2.4 73.9 1.0 OD2 A:ASP207 3.5 85.7 1.0 OG1 A:THR107 3.5 55.7 1.0 PB A:ADP901 3.7 78.4 1.0 OD1 A:ASP207 3.9 86.9 1.0 OE2 A:GLU208 3.9 0.9 1.0 O3A A:ADP901 3.9 76.9 1.0 CG A:ASP207 4.1 90.6 1.0 O2A A:ADP901 4.2 95.0 1.0 O A:GLY490 4.2 0.5 1.0 O1A A:ADP901 4.2 75.7 1.0 PA A:ADP901 4.3 95.7 1.0 CA A:GLY490 4.4 0.2 1.0 CB A:LYS106 4.4 82.6 1.0 O2B A:ADP901 4.5 78.7 1.0 CE A:LYS106 4.5 69.9 1.0 N A:THR107 4.5 77.8 1.0 CD A:GLU208 4.8 0.6 1.0 O3B A:ADP901 4.8 74.2 1.0 C A:GLY490 4.8 0.9 1.0 CB A:THR107 4.9 66.6 1.0

J.F.Hunt, S.Weinkauf, L.Henry, J.J.Fak, P.Mcnicholas, D.B.Oliver, J.Deisenhofer. Nucleotide Control of Interdomain Interactions in the Conformational Reaction Cycle of Seca Science V. 297 2018 2002.
ISSN: ISSN 0036-8075
PubMed: 12242434
DOI: 10.1126/SCIENCE.1074424