Magnesium in PDB 3cz4: Native Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli

All present enzymatic activity of Native Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli:
3.1.3.2;

The structure of Native Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli, PDB code: 3cz4 was solved by R.Leone, E.Cappelletti, M.Benvenuti, G.Lentini, M.C.Thaller, S.Mangani, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	7.99 / 1.70
Space group	I 2 2 2
Cell size a, b, c (Å), α, β, γ (°)	49.294, 92.775, 137.600, 90.00, 90.00, 90.00
R / Rfree (%)	18.1 / 21.2

The structure of Native Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli also contains other interesting chemical elements:

Chlorine

(Cl)

1 atom

The binding sites of Magnesium atom in the Native Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli (pdb code 3cz4). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Native Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli, PDB code: 3cz4:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Native Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 1 of Native Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg213 b:7.2 occ:1.00 O A:HOH485 2.0 16.5 1.0 O A:HOH447 2.0 19.6 1.0 OD2 A:ASP44 2.1 14.4 1.0 O A:HOH279 2.1 16.0 1.0 OD1 A:ASP167 2.1 13.3 1.0 O A:ASP46 2.1 12.2 1.0 CG A:ASP44 3.0 14.4 1.0 CG A:ASP167 3.1 11.9 1.0 C A:ASP46 3.3 12.8 1.0 OD1 A:ASP44 3.4 15.1 1.0 OD2 A:ASP167 3.4 14.6 1.0 OG A:SER168 3.9 12.7 0.5 OG1 A:THR48 4.0 12.6 1.0 CA A:ASP46 4.0 13.4 1.0 N A:ASP46 4.1 13.1 1.0 OD2 A:ASP171 4.1 18.7 1.0 CB A:ASP46 4.2 14.2 1.0 O A:HOH308 4.3 20.4 1.0 CB A:ASP44 4.4 13.6 1.0 N A:ASP47 4.4 11.8 1.0 CB A:ASP167 4.5 11.2 1.0 CH3 A:ACT214 4.5 29.4 1.0 CB A:ASP47 4.6 11.6 1.0 C A:ACT214 4.6 29.2 1.0 N A:ASP167 4.7 11.5 1.0 O A:HOH233 4.7 16.0 1.0 N A:THR48 4.7 11.4 1.0 O A:ACT214 4.8 28.6 1.0 CA A:ASP47 4.8 11.6 1.0 N A:SER168 4.8 13.1 1.0 C A:ASP47 4.8 11.2 1.0 C A:ILE45 4.9 12.9 1.0 CB A:SER168 4.9 13.3 0.5 CB A:SER168 4.9 13.8 0.5 CB A:THR48 5.0 12.2 1.0

Magnesium binding site 2 out of 2 in the Native Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Native Apha Class B Acid Phosphatase/Phosphotransferase From E. Coli within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg216 b:43.0 occ:0.50 O A:HOH530 2.2 26.4 1.0 O A:HOH527 2.2 12.8 1.0 OD1 A:ASN190 3.4 10.3 1.0 CG A:ASN190 3.7 9.3 1.0 CL A:CL215 3.7 23.0 0.5 CB A:ALA188 3.9 9.5 1.0 ND2 A:ASN190 3.9 8.5 1.0 OG A:SER189 3.9 11.9 1.0 N A:SER189 4.1 10.1 1.0 N A:ASN190 4.3 9.1 1.0 CA A:ALA188 4.5 9.3 1.0 CB A:ASN190 4.6 10.2 1.0 C A:ALA188 4.7 9.7 1.0 CA A:SER189 4.9 9.8 1.0 CB A:SER189 5.0 10.9 1.0

R.Leone, E.Cappelletti, M.Benvenuti, G.Lentini, M.C.Thaller, S.Mangani. Structural Insights Into the Catalytic Mechanism of the Bacterial Class B Phosphatase Apha Belonging to the Dddd Superfamily of Phosphohydrolases. J.Mol.Biol. V. 384 478 2008.
ISSN: ISSN 0022-2836
PubMed: 18845157
DOI: 10.1016/J.JMB.2008.09.050