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Atomistry » Zinc » PDB 2v1x-2vh3 » 2v8l | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 2v1x-2vh3 » 2v8l » |
Zinc in PDB 2v8l: Carbohydrate-Binding of the Starch Binding Domain of Rhizopus Oryzae Glucoamylase in Complex with Beta- Cyclodextrin and MaltoheptaoseEnzymatic activity of Carbohydrate-Binding of the Starch Binding Domain of Rhizopus Oryzae Glucoamylase in Complex with Beta- Cyclodextrin and Maltoheptaose
All present enzymatic activity of Carbohydrate-Binding of the Starch Binding Domain of Rhizopus Oryzae Glucoamylase in Complex with Beta- Cyclodextrin and Maltoheptaose:
3.2.1.3; Protein crystallography data
The structure of Carbohydrate-Binding of the Starch Binding Domain of Rhizopus Oryzae Glucoamylase in Complex with Beta- Cyclodextrin and Maltoheptaose, PDB code: 2v8l
was solved by
J.-Y.Tung,
Y.-Y.Liu,
Y.-J.Sun,
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 Carbohydrate-Binding of the Starch Binding Domain of Rhizopus Oryzae Glucoamylase in Complex with Beta- Cyclodextrin and Maltoheptaose
(pdb code 2v8l). 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 Carbohydrate-Binding of the Starch Binding Domain of Rhizopus Oryzae Glucoamylase in Complex with Beta- Cyclodextrin and Maltoheptaose, PDB code: 2v8l: Zinc binding site 1 out of 1 in 2v8lGo back to Zinc Binding Sites List in 2v8l
Zinc binding site 1 out
of 1 in the Carbohydrate-Binding of the Starch Binding Domain of Rhizopus Oryzae Glucoamylase in Complex with Beta- Cyclodextrin and Maltoheptaose
Mono view Stereo pair view
Reference:
J.-Y.Tung,
M.D.-T.Chang,
W.-I.Chou,
Y.-Y.Liu,
Y.Yeh,
F.Chang,
S.Lin,
Z.Qiu,
Y.-J.Sun.
Crystal Structures of the Starch-Binding Domain From Rhizopus Oryzae Glucoamylase Reveal A Polysaccharide-Binding Path. Biochem.J. V. 416 27 2008.
Page generated: Wed Dec 16 03:54:41 2020
ISSN: ISSN 0264-6021 PubMed: 18588504 DOI: 10.1042/BJ20080580 |
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