Magnesium in PDB 3ez2: Partition Protein-Adp Complex

The structure of Partition Protein-Adp Complex, PDB code: 3ez2 was solved by M.A.Schumacher, T.D.Dunham, W.Xu, B.Funnell, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	50.94 / 2.05
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.100, 125.900, 148.400, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 23.2

The binding sites of Magnesium atom in the Partition Protein-Adp Complex (pdb code 3ez2). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Partition Protein-Adp Complex, PDB code: 3ez2:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Partition Protein-Adp Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Partition Protein-Adp Complex within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg399 b:29.6 occ:1.00 O A:HOH638 2.1 21.0 1.0 O A:HOH851 2.2 19.7 1.0 O A:HOH853 2.2 19.4 1.0 OG1 A:THR123 2.2 19.7 1.0 O A:HOH852 2.3 21.8 1.0 O2B A:ADP501 2.3 26.5 1.0 PB A:ADP501 3.2 29.7 1.0 O3B A:ADP501 3.3 28.6 1.0 CB A:THR123 3.4 23.1 1.0 N A:THR123 4.0 22.3 1.0 O2A A:ADP501 4.1 25.2 1.0 O3A A:ADP501 4.1 19.6 1.0 O A:HOH801 4.2 26.8 1.0 O A:HOH431 4.2 24.2 1.0 CA A:THR123 4.2 23.1 1.0 OD2 A:ASP251 4.2 23.0 1.0 OD2 A:ASP152 4.3 23.6 1.0 O A:HOH806 4.3 38.2 1.0 OD1 A:ASP251 4.4 22.2 1.0 CG2 A:THR123 4.4 20.9 1.0 O A:SER252 4.5 28.1 1.0 PA A:ADP501 4.6 27.0 1.0 O1B A:ADP501 4.6 30.5 1.0 O A:HOH433 4.6 23.0 1.0 OG A:SER156 4.6 30.3 1.0 CB A:SER156 4.6 25.0 1.0 CG A:ASP251 4.7 24.8 1.0 CB A:LYS122 4.8 26.3 1.0 O1A A:ADP501 4.8 23.0 1.0 CE A:LYS122 5.0 31.0 1.0

Magnesium binding site 2 out of 2 in the Partition Protein-Adp Complex


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Partition Protein-Adp Complex within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg399 b:26.1 occ:1.00 O B:HOH832 2.2 20.3 1.0 OG1 B:THR123 2.2 20.1 1.0 O2B B:ADP502 2.2 22.8 1.0 O B:HOH857 2.2 19.4 1.0 O B:HOH887 2.3 25.9 1.0 O B:HOH850 2.3 24.2 1.0 PB B:ADP502 3.2 24.7 1.0 CB B:THR123 3.2 23.4 1.0 O3B B:ADP502 3.3 30.9 1.0 N B:THR123 3.9 22.7 1.0 O2A B:ADP502 4.0 25.2 1.0 CA B:THR123 4.1 20.1 1.0 O3A B:ADP502 4.1 20.7 1.0 OD2 B:ASP152 4.1 19.5 1.0 OD2 B:ASP251 4.2 20.9 1.0 O B:HOH876 4.3 32.1 1.0 CG2 B:THR123 4.3 21.6 1.0 O B:HOH455 4.3 24.2 1.0 OD1 B:ASP251 4.3 22.6 1.0 O B:HOH564 4.4 30.8 1.0 PA B:ADP502 4.5 24.8 1.0 O B:HOH530 4.5 21.6 1.0 O1B B:ADP502 4.6 31.9 1.0 OG B:SER156 4.6 32.8 1.0 CB B:SER156 4.6 26.5 1.0 O B:SER252 4.7 24.9 1.0 CB B:LYS122 4.7 13.7 1.0 O1A B:ADP502 4.7 23.1 1.0 CG B:ASP251 4.7 23.3 1.0 C B:LYS122 4.9 18.7 1.0 O B:HOH874 5.0 32.9 1.0 CE B:LYS122 5.0 27.3 1.0

T.D.Dunham, W.Xu, B.E.Funnell, M.A.Schumacher. Structural Basis For Adp-Mediated Transcriptional Regulation By P1 and P7 Para. Embo J. V. 28 1792 2009.
ISSN: ISSN 0261-4189
PubMed: 19461582
DOI: 10.1038/EMBOJ.2009.120