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Atomistry » Zinc » PDB 3h67-3hi2 » 3hgz | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 3h67-3hi2 » 3hgz » |
Zinc in PDB 3hgz: Crystal Structure of Human Insulin-Degrading Enzyme in Complex with AmylinEnzymatic activity of Crystal Structure of Human Insulin-Degrading Enzyme in Complex with Amylin
All present enzymatic activity of Crystal Structure of Human Insulin-Degrading Enzyme in Complex with Amylin:
3.4.24.56; Protein crystallography data
The structure of Crystal Structure of Human Insulin-Degrading Enzyme in Complex with Amylin, PDB code: 3hgz
was solved by
Q.Guo,
Y.Bian,
W.J.Tang,
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 Crystal Structure of Human Insulin-Degrading Enzyme in Complex with Amylin
(pdb code 3hgz). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Human Insulin-Degrading Enzyme in Complex with Amylin, PDB code: 3hgz: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 3hgzGo back to Zinc Binding Sites List in 3hgz
Zinc binding site 1 out
of 2 in the Crystal Structure of Human Insulin-Degrading Enzyme in Complex with Amylin
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 3hgzGo back to Zinc Binding Sites List in 3hgz
Zinc binding site 2 out
of 2 in the Crystal Structure of Human Insulin-Degrading Enzyme in Complex with Amylin
Mono view Stereo pair view
Reference:
Q.Guo,
M.Manolopoulou,
Y.Bian,
A.B.Schilling,
W.J.Tang.
Molecular Basis For the Recognition and Cleavages of Igf-II, Tgf-Alpha, and Amylin By Human Insulin-Degrading Enzyme. J.Mol.Biol. V. 395 430 2010.
Page generated: Thu Oct 24 14:26:57 2024
ISSN: ISSN 0022-2836 PubMed: 19896952 DOI: 10.1016/J.JMB.2009.10.072 |
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