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Atomistry » Zinc » PDB 2y7e-2yql » 2yhg | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 2y7e-2yql » 2yhg » |
Zinc in PDB 2yhg: Ab Initio Phasing of A Nucleoside Hydrolase-Related Hypothetical Protein From Saccharophagus Degradans That Is Associated with Carbohydrate MetabolismProtein crystallography data
The structure of Ab Initio Phasing of A Nucleoside Hydrolase-Related Hypothetical Protein From Saccharophagus Degradans That Is Associated with Carbohydrate Metabolism, PDB code: 2yhg
was solved by
J.H.Hehemann,
C.Marsters,
A.B.Boraston,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2yhg:
The structure of Ab Initio Phasing of A Nucleoside Hydrolase-Related Hypothetical Protein From Saccharophagus Degradans That Is Associated with Carbohydrate Metabolism also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Ab Initio Phasing of A Nucleoside Hydrolase-Related Hypothetical Protein From Saccharophagus Degradans That Is Associated with Carbohydrate Metabolism
(pdb code 2yhg). 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 Ab Initio Phasing of A Nucleoside Hydrolase-Related Hypothetical Protein From Saccharophagus Degradans That Is Associated with Carbohydrate Metabolism, PDB code: 2yhg: Zinc binding site 1 out of 1 in 2yhgGo back to Zinc Binding Sites List in 2yhg
Zinc binding site 1 out
of 1 in the Ab Initio Phasing of A Nucleoside Hydrolase-Related Hypothetical Protein From Saccharophagus Degradans That Is Associated with Carbohydrate Metabolism
Mono view Stereo pair view
Reference:
J.H.Hehemann,
C.Marsters,
A.B.Boraston.
Ab Initio Phasing of A Nucleoside Hydrolase-Related Hypothetical Protein From Saccharophagus Degradans That Is Associated with Carbohydrate Metabolism. Proteins V. 79 2992 2011.
Page generated: Thu Oct 17 05:49:44 2024
ISSN: ESSN 1097-0134 PubMed: 21905122 DOI: 10.1002/PROT.23126 |
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