Magnesium in PDB 3slr: Crystal Structure of N-Terminal Part of the Protein BF1531 From Bacteroides Fragilis Containing Phosphatase Domain Complexed with Mg.

The structure of Crystal Structure of N-Terminal Part of the Protein BF1531 From Bacteroides Fragilis Containing Phosphatase Domain Complexed with Mg., PDB code: 3slr was solved by A.A.Fedorov, E.V.Fedorov, R.Toro, S.K.Burley, S.C.Almo, New York Sgxresearch Center For Structural Genomics (Nysgxrc), with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	37.87 / 1.71
Space group	P 21 21 2
Cell size a, b, c (Å), α, β, γ (°)	75.741, 125.998, 41.622, 90.00, 90.00, 90.00
R / Rfree (%)	18.6 / 21.3

The binding sites of Magnesium atom in the Crystal Structure of N-Terminal Part of the Protein BF1531 From Bacteroides Fragilis Containing Phosphatase Domain Complexed with Mg. (pdb code 3slr). This binding sites where shown within 5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of N-Terminal Part of the Protein BF1531 From Bacteroides Fragilis Containing Phosphatase Domain Complexed with Mg., PDB code: 3slr:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of N-Terminal Part of the Protein BF1531 From Bacteroides Fragilis Containing Phosphatase Domain Complexed with Mg.


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 N-Terminal Part of the Protein BF1531 From Bacteroides Fragilis Containing Phosphatase Domain Complexed with Mg. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg388 b:25.9 occ:1.00 OD1 A:ASP336 2.1 20.5 1.0 O A:HOH662 2.2 26.2 1.0 OD2 A:ASP228 2.2 20.6 1.0 O A:ASP230 2.3 18.8 1.0 O A:HOH492 2.4 26.3 1.0 O A:HOH590 2.5 27.5 1.0 CG A:ASP336 3.1 22.2 1.0 CG A:ASP228 3.2 19.7 1.0 C A:ASP230 3.5 19.9 1.0 OD2 A:ASP336 3.5 23.4 1.0 OD1 A:ASP228 3.5 19.6 1.0 MG A:MG389 3.6 14.1 1.0 OD1 A:ASP335 3.9 21.7 1.0 OG1 A:THR232 4.0 18.9 1.0 CA A:ASP230 4.1 21.3 1.0 CB A:ASP230 4.1 21.6 1.0 N A:ASP230 4.2 18.9 1.0 CB A:ASP336 4.4 17.6 1.0 CB A:ASP228 4.5 18.4 1.0 CB A:ASN231 4.5 18.8 1.0 N A:ASN231 4.5 18.4 1.0 N A:ASP336 4.6 17.2 1.0 O A:HOH660 4.6 23.2 1.0 O A:HOH663 4.7 21.0 1.0 N A:ASN337 4.8 19.0 1.0 CG A:ASP335 4.8 21.1 1.0 C A:ASN231 4.8 17.0 1.0 CA A:ASN231 4.8 17.7 1.0 N A:THR232 4.8 16.9 1.0 O A:HOH661 4.8 30.8 1.0 C A:LEU229 4.9 17.7 1.0 CB A:ASN337 4.9 19.9 1.0 CA A:ASP336 5.0 19.7 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of N-Terminal Part of the Protein BF1531 From Bacteroides Fragilis Containing Phosphatase Domain Complexed with Mg.


Mono view


Stereo pair view

A full contact list of Magnesium with other atoms in the Mg binding site number 2 of Crystal Structure of N-Terminal Part of the Protein BF1531 From Bacteroides Fragilis Containing Phosphatase Domain Complexed with Mg. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg389 b:14.1 occ:1.00 O A:HOH663 1.9 21.0 1.0 O A:HOH660 2.2 23.2 1.0 O A:HOH662 2.2 26.2 1.0 O A:HOH661 2.3 30.8 1.0 OD1 A:ASP228 2.4 19.6 1.0 CG A:ASP228 3.3 19.7 1.0 OD2 A:ASP228 3.6 20.6 1.0 MG A:MG388 3.6 25.9 1.0 OG A:SER279 3.6 19.2 1.0 N A:ASP230 3.8 18.9 1.0 O A:HOH492 3.9 26.3 1.0 CB A:ASP230 3.9 21.6 1.0 N A:LYS280 4.0 18.1 1.0 OD2 A:ASP230 4.1 21.7 1.0 O A:HOH507 4.1 30.3 1.0 NZ A:LYS313 4.2 18.2 1.0 N A:LEU229 4.3 14.2 1.0 O A:LYS280 4.3 24.4 1.0 OD1 A:ASN281 4.3 23.6 1.0 CG A:ASP230 4.4 20.6 1.0 CA A:ASP230 4.4 21.3 1.0 CB A:SER279 4.4 20.8 1.0 CA A:SER279 4.5 18.4 1.0 O A:ASP230 4.5 18.8 1.0 CB A:LYS280 4.6 23.5 1.0 O A:HOH553 4.7 32.2 1.0 CB A:ASP228 4.7 18.4 1.0 C A:LEU229 4.7 17.7 1.0 C A:SER279 4.7 19.8 1.0 CA A:LYS280 4.7 20.2 1.0 C A:LYS280 4.8 22.6 1.0 CA A:LEU229 4.9 18.0 1.0 C A:ASP230 5.0 19.9 1.0

A.A.Fedorov, E.V.Fedorov, R.Toro, S.K.Burley, S.C.Almo. Crystal Structure of N-Terminal Part of the Protein BF1531 From Bacteroides Fragilis Containing Phosphatase Domain Complexed with Mg. To Be Published.