Magnesium in PDB 1ydf: Crystal Structure of A Had-Like Phosphatase From Streptococcus Pneumoniae

The structure of Crystal Structure of A Had-Like Phosphatase From Streptococcus Pneumoniae, PDB code: 1ydf was solved by J.Seetharaman, S.Swaminathan, S.K.Burley, New York Sgx Research Centerfor Structural Genomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	41.49 / 2.60
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	74.430, 99.929, 39.841, 90.00, 90.00, 90.00
R / Rfree (%)	21.7 / 26.7

The binding sites of Magnesium atom in the Crystal Structure of A Had-Like Phosphatase From Streptococcus Pneumoniae (pdb code 1ydf). 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 A Had-Like Phosphatase From Streptococcus Pneumoniae, PDB code: 1ydf:

Magnesium binding site 1 out of 1 in the Crystal Structure of A Had-Like Phosphatase From Streptococcus Pneumoniae


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 Had-Like Phosphatase From Streptococcus Pneumoniae within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg500 b:39.2 occ:1.00 O A:HOH585 1.9 40.0 1.0 O A:HOH586 2.0 43.1 1.0 O A:ASP12 2.4 32.9 1.0 O A:HOH538 2.6 56.7 1.0 OD2 A:ASP207 2.6 42.2 1.0 OD1 A:ASP10 2.6 38.9 1.0 CG A:ASP207 3.4 41.4 1.0 C A:ASP12 3.4 31.3 1.0 CG A:ASP10 3.4 39.7 1.0 OD1 A:ASP207 3.5 41.8 1.0 OD2 A:ASP10 3.5 41.1 1.0 CB A:ASP12 4.1 35.1 1.0 CA A:ASP12 4.1 32.5 1.0 OD2 A:ASP212 4.3 49.7 1.0 N A:ASP12 4.4 32.9 1.0 N A:GLY13 4.4 30.1 1.0 O A:HOH507 4.5 20.0 1.0 CA A:GLY13 4.6 29.7 1.0 OD2 A:ASP12 4.6 41.2 1.0 O A:HOH517 4.6 25.5 1.0 O A:HOH564 4.7 46.1 1.0 CG A:ASP12 4.8 39.3 1.0 CB A:ASP207 4.9 38.3 1.0 CB A:ASP10 4.9 38.5 1.0 CB A:ASN208 4.9 38.2 1.0

J.Seetharaman, S.Swaminathan. Crystal Structure of A Hypothetical Protein, Hydrolase Haloacid Dehalogenase-Like Family To Be Published.