Magnesium in PDB 2uyr: Crystal Structure of Bacillus Cereus Sphingomyelinase Mutant :N57A

All present enzymatic activity of Crystal Structure of Bacillus Cereus Sphingomyelinase Mutant :N57A:
3.1.4.12;

The structure of Crystal Structure of Bacillus Cereus Sphingomyelinase Mutant :N57A, PDB code: 2uyr was solved by M.Oda, H.Tsuge, J.Sakurai, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	54.15 / 2.40
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	55.090, 63.927, 101.690, 90.00, 90.00, 90.00
R / Rfree (%)	18.2 / 23.5

The binding sites of Magnesium atom in the Crystal Structure of Bacillus Cereus Sphingomyelinase Mutant :N57A (pdb code 2uyr). 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 Bacillus Cereus Sphingomyelinase Mutant :N57A, PDB code: 2uyr:

Magnesium binding site 1 out of 1 in the Crystal Structure of Bacillus Cereus Sphingomyelinase Mutant :N57A


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 Bacillus Cereus Sphingomyelinase Mutant :N57A within 5.0Å range: probe atom residue distance (Å) B Occ X:Mg1306 b:18.6 occ:1.00 O X:HOH2084 2.0 19.2 1.0 O X:HOH2010 2.1 10.2 1.0 O X:HOH2086 2.1 15.2 1.0 O X:HOH2009 2.1 17.6 1.0 O X:HOH2083 2.2 13.3 1.0 OE1 X:GLU53 2.3 20.6 1.0 CD X:GLU53 3.2 21.9 1.0 OE2 X:GLU53 3.4 20.6 1.0 OD2 X:ASP295 4.1 14.2 1.0 O X:HOH2026 4.2 44.2 1.0 ND2 X:ASN16 4.2 11.4 1.0 CD1 X:TYR18 4.3 18.7 1.0 O X:HOH2002 4.4 37.3 1.0 OD1 X:ASP295 4.4 15.8 1.0 NE2 X:HIS296 4.5 11.9 1.0 OD1 X:ASN16 4.5 14.1 1.0 CG X:GLU53 4.6 17.4 1.0 CG X:ASP295 4.7 15.0 1.0 CD2 X:HIS296 4.7 10.3 1.0 CE1 X:TYR18 4.8 19.4 1.0 CG X:ASN16 4.8 13.6 1.0 O X:HOH2048 4.8 20.4 1.0 O X:HOH2032 4.8 22.9 1.0 O X:HOH2035 5.0 29.3 1.0

M.Oda, H.Tsuge, J.Sakurai. Crystal Structure of Bacillus Cereus Sphingomyelinase Mutant : N57A To Be Published.