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Atomistry » Calcium » PDB 7c4h-7cgy » 7cgt | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Calcium » PDB 7c4h-7cgy » 7cgt » |
Calcium in PDB 7cgt: Rameb Complex of Cyclodextrin Glycosyltransferase MutantEnzymatic activity of Rameb Complex of Cyclodextrin Glycosyltransferase Mutant
All present enzymatic activity of Rameb Complex of Cyclodextrin Glycosyltransferase Mutant:
2.4.1.19; Protein crystallography data
The structure of Rameb Complex of Cyclodextrin Glycosyltransferase Mutant, PDB code: 7cgt
was solved by
G.Parsiegla,
G.E.Schulz,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Calcium Binding Sites:
The binding sites of Calcium atom in the Rameb Complex of Cyclodextrin Glycosyltransferase Mutant
(pdb code 7cgt). This binding sites where shown within
5.0 Angstroms radius around Calcium atom.
In total 2 binding sites of Calcium where determined in the Rameb Complex of Cyclodextrin Glycosyltransferase Mutant, PDB code: 7cgt: Jump to Calcium binding site number: 1; 2; Calcium binding site 1 out of 2 in 7cgtGo back to Calcium Binding Sites List in 7cgt
Calcium binding site 1 out
of 2 in the Rameb Complex of Cyclodextrin Glycosyltransferase Mutant
Mono view Stereo pair view
Calcium binding site 2 out of 2 in 7cgtGo back to Calcium Binding Sites List in 7cgt
Calcium binding site 2 out
of 2 in the Rameb Complex of Cyclodextrin Glycosyltransferase Mutant
Mono view Stereo pair view
Reference:
G.Parsiegla,
A.K.Schmidt,
G.E.Schulz.
Substrate Binding to A Cyclodextrin Glycosyltransferase and Mutations Increasing the Gamma-Cyclodextrin Production. Eur.J.Biochem. V. 255 710 1998.
Page generated: Thu Jul 18 23:41:46 2024
ISSN: ISSN 0014-2956 PubMed: 9738912 DOI: 10.1046/J.1432-1327.1998.2550710.X |
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