Atomistry » Calcium » PDB 2cn6-2dbx » 2dbx
Atomistry »
  Calcium »
    PDB 2cn6-2dbx »
      2dbx »

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: Fri Jul 12 09:44:05 2024

Last articles

Zn in 9JPJ
Zn in 9JP7
Zn in 9JPK
Zn in 9JPL
Zn in 9GN6
Zn in 9GN7
Zn in 9GKU
Zn in 9GKW
Zn in 9GKX
Zn in 9GL0
© Copyright 2008-2020 by atomistry.com
Home   |    Site Map   |    Copyright   |    Contact us   |    Privacy