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Atomistry » Zinc » PDB 3eyl-3f7i » 3eyx | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 3eyl-3f7i » 3eyx » |
Zinc in PDB 3eyx: Crystal Structure of Carbonic Anhydrase NCE103 From Saccharomyces CerevisiaeEnzymatic activity of Crystal Structure of Carbonic Anhydrase NCE103 From Saccharomyces Cerevisiae
All present enzymatic activity of Crystal Structure of Carbonic Anhydrase NCE103 From Saccharomyces Cerevisiae:
4.2.1.1; Protein crystallography data
The structure of Crystal Structure of Carbonic Anhydrase NCE103 From Saccharomyces Cerevisiae, PDB code: 3eyx
was solved by
Y.B.Teng,
Y.L.Jiang,
Y.Chen,
C.Z.Zhou,
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 Carbonic Anhydrase NCE103 From Saccharomyces Cerevisiae
(pdb code 3eyx). 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 Carbonic Anhydrase NCE103 From Saccharomyces Cerevisiae, PDB code: 3eyx: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 3eyxGo back to Zinc Binding Sites List in 3eyx
Zinc binding site 1 out
of 2 in the Crystal Structure of Carbonic Anhydrase NCE103 From Saccharomyces Cerevisiae
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 3eyxGo back to Zinc Binding Sites List in 3eyx
Zinc binding site 2 out
of 2 in the Crystal Structure of Carbonic Anhydrase NCE103 From Saccharomyces Cerevisiae
Mono view Stereo pair view
Reference:
Y.B.Teng,
Y.L.Jiang,
Y.X.He,
W.W.He,
F.M.Lian,
Y.Chen,
C.Z.Zhou.
Structural Insights Into the Substrate Tunnel of Saccharomyces Cerevisiae Carbonic Anhydrase NCE103. Bmc Struct.Biol. V. 9 67 2009.
Page generated: Wed Dec 16 04:17:19 2020
ISSN: ESSN 1472-6807 PubMed: 19852838 DOI: 10.1186/1472-6807-9-67 |
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