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Calcium in PDB 2dbx: Crystal Structure of Gamma-Glutamyltranspeptidase From Escherichia Coli Complexed with L-Glutamate

Enzymatic activity of Crystal Structure of Gamma-Glutamyltranspeptidase From Escherichia Coli Complexed with L-Glutamate

All present enzymatic activity of Crystal Structure of Gamma-Glutamyltranspeptidase From Escherichia Coli Complexed with L-Glutamate:
2.3.2.2;

Protein crystallography data

The structure of Crystal Structure of Gamma-Glutamyltranspeptidase From Escherichia Coli Complexed with L-Glutamate, PDB code: 2dbx 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) 46.24 / 1.70
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 77.700, 126.500, 129.200, 90.00, 90.00, 90.00
R / Rfree (%) 19.4 / 21.2

Calcium Binding Sites:

The binding sites of Calcium atom in the Crystal Structure of Gamma-Glutamyltranspeptidase From Escherichia Coli Complexed with L-Glutamate (pdb code 2dbx). 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 Complexed with L-Glutamate, PDB code: 2dbx:
Jump to Calcium binding site number: 1; 2;

Calcium binding site 1 out of 2 in 2dbx

Go back to Calcium Binding Sites List in 2dbx
Calcium binding site 1 out of 2 in the Crystal Structure of Gamma-Glutamyltranspeptidase From Escherichia Coli Complexed with L-Glutamate


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 Complexed with L-Glutamate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:Ca701

b:25.0
occ:1.00
O B:HOH1792 2.4 28.9 1.0
O B:SER572 2.4 23.9 1.0
O B:HOH1791 2.4 25.4 1.0
O B:ASP569 2.5 20.2 1.0
OD1 B:ASP575 2.5 26.9 1.0
OD2 B:ASP575 2.8 24.8 1.0
CG B:ASP575 3.0 24.4 1.0
C B:ASP569 3.5 19.6 1.0
C B:SER572 3.6 24.1 1.0
CA B:PRO570 4.0 19.1 1.0
O B:HOH1234 4.2 28.1 1.0
N B:PRO570 4.2 19.4 1.0
C B:PRO570 4.2 19.4 1.0
O B:PRO570 4.3 19.8 1.0
N B:SER572 4.4 20.3 1.0
CA B:VAL573 4.4 23.1 1.0
N B:VAL573 4.4 23.2 1.0
OG B:SER572 4.4 31.5 1.0
CB B:ASP575 4.4 22.4 1.0
CA B:SER572 4.5 23.4 1.0
N B:ASP569 4.5 21.8 1.0
CB B:SER568 4.5 20.0 1.0
CA B:ASP569 4.6 20.2 1.0
C B:SER568 4.6 20.5 1.0
O B:SER568 4.6 25.1 1.0
N B:ASP575 4.8 22.6 1.0
C B:VAL573 4.9 22.3 1.0
N B:ARG571 5.0 20.1 1.0
CB B:SER572 5.0 25.5 1.0

Calcium binding site 2 out of 2 in 2dbx

Go back to Calcium Binding Sites List in 2dbx
Calcium binding site 2 out of 2 in the Crystal Structure of Gamma-Glutamyltranspeptidase From Escherichia Coli Complexed with L-Glutamate


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 Complexed with L-Glutamate within 5.0Å range:
probe atom residue distance (Å) B Occ
D:Ca702

b:24.2
occ:1.00
O D:HOH1795 2.3 30.1 1.0
O D:HOH1793 2.4 27.8 1.0
O D:HOH1794 2.4 28.3 1.0
O D:ASP569 2.4 20.2 1.0
O D:SER572 2.4 26.5 1.0
OD1 D:ASP575 2.5 24.7 1.0
OD2 D:ASP575 2.8 23.3 1.0
CG D:ASP575 3.0 24.6 1.0
C D:ASP569 3.5 19.7 1.0
C D:SER572 3.6 24.2 1.0
CA D:PRO570 3.9 20.0 1.0
O D:HOH1218 4.1 30.3 1.0
N D:PRO570 4.1 19.0 1.0
C D:PRO570 4.2 20.1 1.0
OG D:SER572 4.2 32.9 1.0
O D:PRO570 4.3 21.1 1.0
N D:SER572 4.3 22.2 1.0
CA D:SER572 4.4 24.1 1.0
N D:VAL573 4.5 23.6 1.0
CB D:ASP575 4.5 20.5 1.0
CA D:VAL573 4.5 24.5 1.0
N D:ASP569 4.5 20.4 1.0
CA D:ASP569 4.5 20.2 1.0
CB D:SER568 4.6 18.7 1.0
C D:SER568 4.6 20.3 1.0
O D:SER568 4.7 23.3 1.0
N D:ASP575 4.8 21.4 1.0
CB D:SER572 4.9 27.0 1.0
N D:ARG571 4.9 21.6 1.0
C D:VAL573 5.0 24.1 1.0

Reference:

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
Page generated: Tue Jul 8 05:00:18 2025

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