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Atomistry » Fluorine » PDB 3g72-3gwv » 3ghh » |
Fluorine in PDB 3ghh: Structural Insights Into the Catalytic Mechanism of CD38: Evidence For A Conformationally Flexible Covalent Enzyme-Substrate Complex.Enzymatic activity of Structural Insights Into the Catalytic Mechanism of CD38: Evidence For A Conformationally Flexible Covalent Enzyme-Substrate Complex.
All present enzymatic activity of Structural Insights Into the Catalytic Mechanism of CD38: Evidence For A Conformationally Flexible Covalent Enzyme-Substrate Complex.:
3.2.2.5; Protein crystallography data
The structure of Structural Insights Into the Catalytic Mechanism of CD38: Evidence For A Conformationally Flexible Covalent Enzyme-Substrate Complex., PDB code: 3ghh
was solved by
P.F.Egea,
H.Muller-Steffner,
R.M.Stroud,
N.J.Oppenheimer,
E.Kellenberger,
F.Schuber,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Structural Insights Into the Catalytic Mechanism of CD38: Evidence For A Conformationally Flexible Covalent Enzyme-Substrate Complex.
(pdb code 3ghh). This binding sites where shown within
5.0 Angstroms radius around Fluorine atom.
In total only one binding site of Fluorine was determined in the Structural Insights Into the Catalytic Mechanism of CD38: Evidence For A Conformationally Flexible Covalent Enzyme-Substrate Complex., PDB code: 3ghh: Fluorine binding site 1 out of 1 in 3ghhGo back to Fluorine Binding Sites List in 3ghh
Fluorine binding site 1 out
of 1 in the Structural Insights Into the Catalytic Mechanism of CD38: Evidence For A Conformationally Flexible Covalent Enzyme-Substrate Complex.
Mono view Stereo pair view
Reference:
P.F.Egea,
H.Muller-Steffner,
I.Kuhn,
C.Cakir-Kiefer,
N.J.Oppenheimer,
R.M.Stroud,
E.Kellenberger,
F.Schuber.
Insights Into the Mechanism of Bovine CD38/Nad+Glycohydrolase From the X-Ray Structures of Its Michaelis Complex and Covalently-Trapped Intermediates. Plos One V. 7 34918 2012.
Page generated: Sun Dec 13 11:46:50 2020
ISSN: ESSN 1932-6203 PubMed: 22529956 DOI: 10.1371/JOURNAL.PONE.0034918 |
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