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Atomistry » Zinc » PDB 2hpy-2i7v » 2i3c | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 2hpy-2i7v » 2i3c » |
Zinc in PDB 2i3c: Crystal Structure of An Aspartoacylase From Homo SapiensEnzymatic activity of Crystal Structure of An Aspartoacylase From Homo Sapiens
All present enzymatic activity of Crystal Structure of An Aspartoacylase From Homo Sapiens:
3.5.1.15; Protein crystallography data
The structure of Crystal Structure of An Aspartoacylase From Homo Sapiens, PDB code: 2i3c
was solved by
E.Bitto,
G.E.Wesenberg,
G.N.Phillips Jr.,
J.G.Mccoy,
C.A.Bingman,
Centerfor Eukaryotic Structural Genomics (Cesg),
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 An Aspartoacylase From Homo Sapiens
(pdb code 2i3c). 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 An Aspartoacylase From Homo Sapiens, PDB code: 2i3c: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 2i3cGo back to Zinc Binding Sites List in 2i3c
Zinc binding site 1 out
of 2 in the Crystal Structure of An Aspartoacylase From Homo Sapiens
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 2i3cGo back to Zinc Binding Sites List in 2i3c
Zinc binding site 2 out
of 2 in the Crystal Structure of An Aspartoacylase From Homo Sapiens
Mono view Stereo pair view
Reference:
E.Bitto,
C.A.Bingman,
G.E.Wesenberg,
J.G.Mccoy,
G.N.Phillips.
Structure of Aspartoacylase, the Brain Enzyme Impaired in Canavan Disease. Proc.Natl.Acad.Sci.Usa V. 104 456 2007.
Page generated: Wed Dec 16 03:30:45 2020
ISSN: ISSN 0027-8424 PubMed: 17194761 DOI: 10.1073/PNAS.0607817104 |
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