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Atomistry » Zinc » PDB 6zpf-6zxd » 6zpu | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 6zpf-6zxd » 6zpu » |
Zinc in PDB 6zpu: Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus.Enzymatic activity of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus.
All present enzymatic activity of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus.:
3.4.15.1; Protein crystallography data
The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus., PDB code: 6zpu
was solved by
G.E.Cozier,
K.R.Acharya,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6zpu:
The structure of Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus. also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus.
(pdb code 6zpu). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus., PDB code: 6zpu: Zinc binding site 1 out of 1 in 6zpuGo back to Zinc Binding Sites List in 6zpu
Zinc binding site 1 out
of 1 in the Crystal Structure of Angiotensin-1 Converting Enzyme C-Domain with Inserted Symmetry Molecule C-Terminus.
Mono view Stereo pair view
Reference:
G.E.Cozier,
L.Lubbe,
E.D.Sturrock,
K.R.Acharya.
Angiotensin-Converting Enzyme Open For Business: Structural Insights Into the Sub-Domain Dynamics. Febs J. 2020.
Page generated: Tue Oct 29 15:52:50 2024
ISSN: ISSN 1742-464X PubMed: 33067882 DOI: 10.1111/FEBS.15601 |
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