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Magnesium in PDB 4otu: Crystal Structure of the Gamma-Glutamyltranspeptidase From Bacillus Licheniformis in Complex with L-Glutamate

Enzymatic activity of Crystal Structure of the Gamma-Glutamyltranspeptidase From Bacillus Licheniformis in Complex with L-Glutamate

All present enzymatic activity of Crystal Structure of the Gamma-Glutamyltranspeptidase From Bacillus Licheniformis in Complex with L-Glutamate:
2.3.2.2;

Protein crystallography data

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

Resolution Low / High (Å) 27.99 / 3.02
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 60.627, 60.465, 145.718, 90.00, 90.00, 90.00
R / Rfree (%) 20.2 / 28.8

Magnesium Binding Sites:

The binding sites of Magnesium atom in the Crystal Structure of the Gamma-Glutamyltranspeptidase From Bacillus Licheniformis in Complex with L-Glutamate (pdb code 4otu). 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 the Gamma-Glutamyltranspeptidase From Bacillus Licheniformis in Complex with L-Glutamate, PDB code: 4otu:

Magnesium binding site 1 out of 1 in 4otu

Go back to Magnesium Binding Sites List in 4otu
Magnesium binding site 1 out of 1 in the Crystal Structure of the Gamma-Glutamyltranspeptidase From Bacillus Licheniformis in Complex with L-Glutamate


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 in Complex with L-Glutamate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Mg601

b:16.0
occ:1.00
 OE1 B:GLU523 2.5 29.1 1.0
OD1 B:ASP568 3.0 31.8 1.0
CD B:GLU523 3.4 30.6 1.0
OD2 B:ASP568 3.6 32.0 1.0
OE2 B:GLU523 3.7 31.9 1.0
CG B:ASP568 3.7 33.1 1.0
OE1 B:GLU508 3.9 30.7 1.0
OD1 B:ASP547 4.3 43.4 1.0
O B:ILE507 4.4 28.2 1.0
OG B:SER569 4.4 30.3 1.0
CB B:SER570 4.5 35.5 1.0
N B:SER570 4.6 32.6 1.0
O B:ILE548 4.6 30.1 1.0
O B:GLU508 4.7 29.4 1.0
CA B:GLU508 4.7 28.2 1.0
CG B:GLU523 4.7 31.7 1.0
CD B:GLU508 4.9 31.4 1.0
CA B:SER570 4.9 34.0 1.0
NH2 B:ARG511 4.9 37.1 1.0
C B:GLU508 5.0 29.4 1.0

Reference:

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
Page generated: Tue Aug 20 00:59:47 2024

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