Magnesium in PDB 4ott: Crystal Structure of the Gamma-Glutamyltranspeptidase From Bacillus Licheniformis.

All present enzymatic activity of Crystal Structure of the Gamma-Glutamyltranspeptidase From Bacillus Licheniformis.:
2.3.2.2;

The structure of Crystal Structure of the Gamma-Glutamyltranspeptidase From Bacillus Licheniformis., PDB code: 4ott was solved by A.Merlino, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	26.25 / 2.98
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	60.896, 61.968, 148.245, 90.00, 90.00, 90.00
R / Rfree (%)	19.1 / 25

The binding sites of Magnesium atom in the Crystal Structure of the Gamma-Glutamyltranspeptidase From Bacillus Licheniformis. (pdb code 4ott). 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 the Gamma-Glutamyltranspeptidase From Bacillus Licheniformis., PDB code: 4ott:
Jump to Magnesium binding site number: 1; 2;

Magnesium binding site 1 out of 2 in the Crystal Structure of the Gamma-Glutamyltranspeptidase From Bacillus Licheniformis.


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 the Gamma-Glutamyltranspeptidase From Bacillus Licheniformis. within 5.0Å range: probe atom residue distance (Å) B Occ A:Mg401 b:20.4 occ:1.00 OE2 B:GLU498 1.9 29.4 1.0 NE2 A:HIS277 2.5 28.0 1.0 CD B:GLU498 3.1 30.5 1.0 CE1 A:HIS277 3.2 27.7 1.0 CD2 A:HIS277 3.7 27.8 1.0 OG A:SER307 3.8 31.8 1.0 CG B:GLU498 3.9 31.1 1.0 OE1 B:GLU498 4.0 28.1 1.0 O B:GLU498 4.3 33.0 1.0 ND1 A:HIS277 4.4 27.3 1.0 CA B:GLU498 4.5 30.0 1.0 CG A:HIS277 4.7 27.1 1.0 CB B:GLU498 4.8 30.0 1.0 CD2 A:HIS305 4.8 26.0 1.0 C B:GLU498 4.9 29.9 1.0

Magnesium binding site 2 out of 2 in the Crystal Structure of the Gamma-Glutamyltranspeptidase From Bacillus Licheniformis.


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 the Gamma-Glutamyltranspeptidase From Bacillus Licheniformis. within 5.0Å range: probe atom residue distance (Å) B Occ B:Mg601 b:21.5 occ:1.00 OE1 B:GLU523 2.5 28.9 1.0 OD1 B:ASP568 3.3 35.5 1.0 CD B:GLU523 3.5 27.4 1.0 OE1 B:GLU508 3.7 29.3 1.0 OE2 B:GLU523 3.8 29.4 1.0 O B:GLU508 4.0 27.9 1.0 OD2 B:ASP568 4.0 37.0 1.0 OG B:SER569 4.0 29.9 1.0 CG B:ASP568 4.0 35.9 1.0 O B:ILE507 4.2 24.1 1.0 CA B:GLU508 4.2 28.2 1.0 CD B:GLU508 4.3 29.9 1.0 OE2 B:GLU508 4.4 32.3 1.0 C B:GLU508 4.5 28.3 1.0 NH2 B:ARG511 4.8 28.8 1.0 CG B:GLU523 4.9 24.6 1.0 CB B:SER570 4.9 26.5 1.0 N B:SER570 4.9 25.7 1.0 C B:ILE507 4.9 25.6 1.0

L.L.Lin, Y.Y.Chen, M.C.Chi, A.Merlino. Low Resolution X-Ray Structure of Gamma-Glutamyltranspeptidase From Bacillus Licheniformis: Opened Active Site Cleft and A Cluster of Acid Residues Potentially Involved in the Recognition of A Metal Ion. Biochim.Biophys.Acta V.1844 1523 2014.
ISSN: ISSN 0006-3002
PubMed: 24780583
DOI: 10.1016/J.BBAPAP.2014.04.016