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Atomistry » Calcium » PDB 2cn6-2dbx » 2dbx » |
Calcium in PDB 2dbx: Crystal Structure of Gamma-Glutamyltranspeptidase From Escherichia Coli Complexed with L-GlutamateEnzymatic 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:
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 2dbxGo 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
Calcium binding site 2 out of 2 in 2dbxGo 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
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.
Page generated: Fri Jul 12 09:44:05 2024
ISSN: ISSN 0027-8424 PubMed: 16618936 DOI: 10.1073/PNAS.0511020103 |
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