Magnesium in PDB 1tf2: Crystal Structure of Seca:Adp in An Open Conformation From Bacillus Subtilis

The structure of Crystal Structure of Seca:Adp in An Open Conformation From Bacillus Subtilis, PDB code: 1tf2 was solved by A.R.Osborne, W.M.Clemons Jr., T.A.Rapoport, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	44.98 / 2.90
Space group	C 1 2 1
Cell size a, b, c (Å), α, β, γ (°)	149.232, 107.189, 72.054, 90.00, 94.96, 90.00
R / Rfree (%)	22.8 / 29.2

The binding sites of Magnesium atom in the Crystal Structure of Seca:Adp in An Open Conformation From Bacillus Subtilis (pdb code 1tf2). 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 Seca:Adp in An Open Conformation From Bacillus Subtilis, PDB code: 1tf2:

Magnesium binding site 1 out of 1 in the Crystal Structure of Seca:Adp in An Open Conformation 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 Seca:Adp in An Open Conformation From Bacillus Subtilis within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg842 b:41.2 occ:1.00 O A:HOH2008 2.0 21.8 1.0 O A:HOH2013 2.5 21.5 1.0 O1B A:ADP843 2.6 68.6 1.0 OD2 A:ASP207 3.0 43.9 1.0 OD1 A:ASP207 3.5 40.5 1.0 CG A:ASP207 3.7 38.3 1.0 OG1 A:THR107 3.8 39.8 1.0 PB A:ADP843 4.1 68.5 1.0 CB A:LYS106 4.2 41.6 1.0 O1A A:ADP843 4.4 65.3 1.0 OE2 A:GLU208 4.4 47.4 1.0 NZ A:LYS106 4.6 44.2 1.0 N A:THR107 4.6 42.1 1.0 O2B A:ADP843 4.8 68.6 1.0 CD A:LYS106 4.8 42.2 1.0 O3A A:ADP843 4.8 68.6 1.0 CA A:GLY490 4.8 47.5 1.0 O3B A:ADP843 4.9 69.0 1.0 CE A:MET370 4.9 54.1 1.0 CD A:GLU208 5.0 45.2 1.0 CB A:THR107 5.0 40.3 1.0 PA A:ADP843 5.0 67.1 1.0

A.R.Osborne, W.M.Clemons Jr., T.A.Rapoport. A Large Conformational Change of the Translocation Atpase Seca. Proc.Natl.Acad.Sci.Usa V. 101 10937 2004.
ISSN: ISSN 0027-8424
PubMed: 15256599
DOI: 10.1073/PNAS.0401742101