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Atomistry » Zinc » PDB 1i96-1im5 » 1ia7 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 1i96-1im5 » 1ia7 » |
Zinc in PDB 1ia7: Crystal Structure of the Cellulase CEL9M of C. Cellulolyticium in Complex with CellobioseEnzymatic activity of Crystal Structure of the Cellulase CEL9M of C. Cellulolyticium in Complex with Cellobiose
All present enzymatic activity of Crystal Structure of the Cellulase CEL9M of C. Cellulolyticium in Complex with Cellobiose:
3.2.1.4; Protein crystallography data
The structure of Crystal Structure of the Cellulase CEL9M of C. Cellulolyticium in Complex with Cellobiose, PDB code: 1ia7
was solved by
G.Parsiegla,
A.Belaich,
J.P.Belaich,
R.Haser,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1ia7:
The structure of Crystal Structure of the Cellulase CEL9M of C. Cellulolyticium in Complex with Cellobiose also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of the Cellulase CEL9M of C. Cellulolyticium in Complex with Cellobiose
(pdb code 1ia7). 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 the Cellulase CEL9M of C. Cellulolyticium in Complex with Cellobiose, PDB code: 1ia7: Zinc binding site 1 out of 1 in 1ia7Go back to Zinc Binding Sites List in 1ia7
Zinc binding site 1 out
of 1 in the Crystal Structure of the Cellulase CEL9M of C. Cellulolyticium in Complex with Cellobiose
Mono view Stereo pair view
Reference:
G.Parsiegla,
A.Belaich,
J.P.Belaich,
R.Haser.
Crystal Structure of the Cellulase CEL9M Enlightens Structure/Function Relationships of the Variable Catalytic Modules in Glycoside Hydrolases. Biochemistry V. 41 11134 2002.
Page generated: Wed Dec 16 02:52:34 2020
ISSN: ISSN 0006-2960 PubMed: 12220178 DOI: 10.1021/BI025816M |
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