Calcium in PDB 2e0x: Crystal Structure of Gamma-Glutamyltranspeptidase From Escherichia Coli (Monoclinic Form)

All present enzymatic activity of Crystal Structure of Gamma-Glutamyltranspeptidase From Escherichia Coli (Monoclinic Form):
2.3.2.2;

The structure of Crystal Structure of Gamma-Glutamyltranspeptidase From Escherichia Coli (Monoclinic Form), PDB code: 2e0x 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)	29.91 / 1.95
Space group	P 1 21 1
Cell size a, b, c (Å), α, β, γ (°)	65.230, 127.900, 75.140, 90.00, 94.78, 90.00
R / Rfree (%)	19.3 / 23.1

The binding sites of Calcium atom in the Crystal Structure of Gamma-Glutamyltranspeptidase From Escherichia Coli (Monoclinic Form) (pdb code 2e0x). 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-Glutamyltranspeptidase From Escherichia Coli (Monoclinic Form), PDB code: 2e0x:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in the Crystal Structure of Gamma-Glutamyltranspeptidase From Escherichia Coli (Monoclinic Form)


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-Glutamyltranspeptidase From Escherichia Coli (Monoclinic Form) within 5.0Å range: probe atom residue distance (Å) B Occ B:Ca701 b:21.1 occ:1.00 OD1 B:ASP575 2.2 15.0 1.0 O B:ASP569 2.3 9.3 1.0 O B:SER572 2.4 13.8 1.0 OD2 B:ASP575 2.8 12.8 1.0 CG B:ASP575 2.8 12.6 1.0 C B:ASP569 3.4 9.6 1.0 C B:SER572 3.6 12.3 1.0 CA B:PRO570 3.9 9.0 1.0 N B:PRO570 4.1 9.1 1.0 O B:HOH1292 4.1 19.5 1.0 C B:PRO570 4.1 9.0 1.0 O B:PRO570 4.2 9.0 1.0 CB B:ASP575 4.3 11.0 1.0 N B:SER572 4.3 10.7 1.0 CA B:SER572 4.4 12.2 1.0 N B:ASP569 4.5 10.4 1.0 CB B:SER568 4.5 10.2 1.0 N B:VAL573 4.5 12.6 1.0 C B:SER568 4.5 10.5 1.0 CA B:ASP569 4.5 10.0 1.0 O B:SER568 4.5 10.5 1.0 CA B:VAL573 4.6 12.8 1.0 CB B:SER572 4.7 12.1 1.0 N B:ASP575 4.7 11.3 1.0 O B:HOH1304 4.8 18.5 1.0 N B:ARG571 4.9 9.3 1.0 CA B:ASP575 4.9 11.4 1.0 C B:VAL573 4.9 12.2 1.0 O B:ASP575 5.0 11.5 1.0

Calcium binding site 2 out of 2 in the Crystal Structure of Gamma-Glutamyltranspeptidase From Escherichia Coli (Monoclinic Form)


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-Glutamyltranspeptidase From Escherichia Coli (Monoclinic Form) within 5.0Å range: probe atom residue distance (Å) B Occ D:Ca702 b:27.7 occ:1.00 OD1 D:ASP575 2.2 14.8 1.0 O D:SER572 2.4 14.0 1.0 O D:ASP569 2.5 10.8 1.0 OD2 D:ASP575 2.9 13.5 1.0 CG D:ASP575 2.9 13.9 1.0 C D:ASP569 3.4 11.0 1.0 C D:SER572 3.6 13.4 1.0 CA D:PRO570 3.8 11.0 1.0 N D:PRO570 4.0 11.1 1.0 C D:PRO570 4.1 10.8 1.0 O D:HOH1220 4.2 15.5 1.0 O D:PRO570 4.2 10.6 1.0 N D:SER572 4.3 12.2 1.0 CB D:ASP575 4.3 12.6 1.0 CA D:SER572 4.4 13.1 1.0 N D:VAL573 4.5 13.0 1.0 CB D:SER568 4.5 11.4 1.0 N D:ASP569 4.6 11.3 1.0 CA D:VAL573 4.6 13.7 1.0 C D:SER568 4.6 11.4 1.0 CA D:ASP569 4.6 10.8 1.0 CB D:SER572 4.6 12.9 1.0 N D:ASP575 4.6 13.0 1.0 O D:SER568 4.7 10.8 1.0 N D:ARG571 4.7 10.5 1.0 O D:HOH1384 4.8 20.6 1.0 CA D:ASP575 4.9 13.0 1.0 C D:VAL573 4.9 13.1 1.0

T.Okada, H.Suzuki, K.Wada, H.Kumagai, K.Fukuyama. Crystal Structure of the Gamma-Glutamyltranspeptidase Precursor Protein From Escherichia Coli. Structural Changes Upon Autocatalytic Processing and Implications For the Maturation Mechanism J.Biol.Chem. V. 282 2433 2007.
ISSN: ISSN 0021-9258
PubMed: 17135273
DOI: 10.1074/JBC.M607490200