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Atomistry » Zinc » PDB 2q1z-2ql1 » 2qg9 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 2q1z-2ql1 » 2qg9 » |
Zinc in PDB 2qg9: Structure of A Regulatory Subunit Mutant D19A of Atcase From E. ColiEnzymatic activity of Structure of A Regulatory Subunit Mutant D19A of Atcase From E. Coli
All present enzymatic activity of Structure of A Regulatory Subunit Mutant D19A of Atcase From E. Coli:
2.1.3.2; Protein crystallography data
The structure of Structure of A Regulatory Subunit Mutant D19A of Atcase From E. Coli, PDB code: 2qg9
was solved by
B.Stec,
M.K.Williams,
K.A.Stieglitz,
E.R.Kantrowitz,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Zinc Binding Sites:
The binding sites of Zinc atom in the Structure of A Regulatory Subunit Mutant D19A of Atcase From E. Coli
(pdb code 2qg9). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of A Regulatory Subunit Mutant D19A of Atcase From E. Coli, PDB code: 2qg9: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 2qg9Go back to Zinc Binding Sites List in 2qg9
Zinc binding site 1 out
of 2 in the Structure of A Regulatory Subunit Mutant D19A of Atcase From E. Coli
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 2qg9Go back to Zinc Binding Sites List in 2qg9
Zinc binding site 2 out
of 2 in the Structure of A Regulatory Subunit Mutant D19A of Atcase From E. Coli
Mono view Stereo pair view
Reference:
B.Stec,
M.K.Williams,
K.A.Stieglitz,
E.R.Kantrowitz.
Comparison of Two T-State Structures of Regulatory-Chain Mutants of Escherichia Coli Aspartate Transcarbamoylase Suggests That HIS20 and ASP19 Modulate the Response to Heterotropic Effectors. Acta Crystallogr.,Sect.D V. 63 1243 2007.
Page generated: Thu Oct 17 03:26:52 2024
ISSN: ISSN 0907-4449 PubMed: 18084072 DOI: 10.1107/S0907444907052985 |
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