Calcium in PDB 2dg5: Crystal Structure of Gamma-Glutamyl Transpeptidase From Escherichia Coli in Complex with Hydrolyzed Glutathione

All present enzymatic activity of Crystal Structure of Gamma-Glutamyl Transpeptidase From Escherichia Coli in Complex with Hydrolyzed Glutathione:
2.3.2.2;

The structure of Crystal Structure of Gamma-Glutamyl Transpeptidase From Escherichia Coli in Complex with Hydrolyzed Glutathione, PDB code: 2dg5 was solved by T.Okada, K.Wada, K.Fukuyama, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å)	46.34 / 1.60
Space group	P 21 21 21
Cell size a, b, c (Å), α, β, γ (°)	78.140, 126.600, 129.200, 90.00, 90.00, 90.00
R / Rfree (%)	17.9 / 19.5

The binding sites of Calcium atom in the Crystal Structure of Gamma-Glutamyl Transpeptidase From Escherichia Coli in Complex with Hydrolyzed Glutathione (pdb code 2dg5). This binding sites where shown within 5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Crystal Structure of Gamma-Glutamyl Transpeptidase From Escherichia Coli in Complex with Hydrolyzed Glutathione, PDB code: 2dg5:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Gamma-Glutamyl Transpeptidase From Escherichia Coli in Complex with Hydrolyzed Glutathione


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 1 of Crystal Structure of Gamma-Glutamyl Transpeptidase From Escherichia Coli in Complex with Hydrolyzed Glutathione within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca701 b:13.7 occ:1.00 O B:HOH1861 2.2 20.8 1.0 O B:HOH1863 2.3 18.6 1.0 O B:HOH1862 2.4 23.5 1.0 O B:SER572 2.4 14.4 1.0 O B:HOH1860 2.4 19.4 1.0 O B:ASP569 2.4 11.9 1.0 OD1 B:ASP575 2.5 15.9 1.0 OD2 B:ASP575 2.9 11.6 1.0 CG B:ASP575 3.0 13.2 1.0 C B:ASP569 3.5 10.9 1.0 C B:SER572 3.5 14.0 1.0 CA B:PRO570 4.0 10.1 1.0 O B:HOH1233 4.1 17.3 1.0 N B:PRO570 4.1 10.7 1.0 OG B:SER572 4.2 25.8 1.0 C B:PRO570 4.2 9.9 1.0 N B:SER572 4.3 12.0 1.0 O B:PRO570 4.3 11.1 1.0 CA B:SER572 4.4 13.9 1.0 N B:VAL573 4.4 13.0 1.0 N B:ASP569 4.4 12.2 1.0 CA B:VAL573 4.4 12.8 1.0 O B:HOH1849 4.4 30.4 1.0 CB B:ASP575 4.5 12.5 1.0 CA B:ASP569 4.5 11.3 1.0 CB B:SER568 4.5 10.0 1.0 O B:HOH1807 4.6 28.9 1.0 C B:SER568 4.6 12.0 1.0 N B:ASP575 4.8 12.7 1.0 O B:SER568 4.8 15.1 1.0 CB B:SER572 4.9 17.8 1.0 C B:VAL573 4.9 12.9 1.0 O C:HOH1764 4.9 26.1 1.0 N B:ARG571 4.9 11.0 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Gamma-Glutamyl Transpeptidase From Escherichia Coli in Complex with Hydrolyzed Glutathione


Mono view


Stereo pair view

A full contact list of Calcium with other atoms in the Ca binding site number 2 of Crystal Structure of Gamma-Glutamyl Transpeptidase From Escherichia Coli in Complex with Hydrolyzed Glutathione within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca702 b:12.9 occ:1.00 O D:HOH1867 2.4 18.2 1.0 O D:ASP569 2.4 11.6 1.0 O D:SER572 2.4 13.5 1.0 O D:HOH1865 2.4 17.4 1.0 O D:HOH1864 2.4 18.1 1.0 OD1 D:ASP575 2.5 14.7 1.0 O D:HOH1866 2.6 21.8 1.0 OD2 D:ASP575 2.9 12.0 1.0 CG D:ASP575 3.0 12.5 1.0 C D:ASP569 3.4 10.9 1.0 C D:SER572 3.5 12.4 1.0 CA D:PRO570 4.0 10.4 1.0 O D:HOH1218 4.1 19.1 1.0 N D:PRO570 4.2 10.2 1.0 OG D:SER572 4.2 18.5 1.0 C D:PRO570 4.2 10.3 1.0 N D:SER572 4.3 11.4 1.0 O D:PRO570 4.3 11.4 1.0 N D:ASP569 4.3 10.7 1.0 N D:VAL573 4.4 12.5 1.0 CA D:VAL573 4.4 13.1 1.0 CA D:SER572 4.4 12.0 1.0 CB D:ASP575 4.4 11.0 1.0 CA D:ASP569 4.4 11.3 1.0 CB D:SER568 4.5 10.9 1.0 O D:HOH1816 4.6 24.1 1.0 C D:SER568 4.7 11.5 1.0 N D:ASP575 4.7 11.9 1.0 CB D:SER572 4.9 15.5 1.0 C D:VAL573 4.9 12.5 1.0 N D:ARG571 4.9 10.8 1.0 O D:SER568 5.0 15.0 1.0

T.Okada, H.Suzuki, K.Wada, H.Kumagai, K.Fukuyama. Crystal Structures of Gamma-Glutamyltranspeptidase From Escherichia Coli, A Key Enzyme in Glutathione Metabolism, and Its Reaction Intermediate. Proc.Natl.Acad.Sci.Usa V. 103 6471 2006.
ISSN: ISSN 0027-8424
PubMed: 16618936
DOI: 10.1073/PNAS.0511020103