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Atomistry » Fluorine » PDB 1bwf-1dvy » 1c5i » |
Fluorine in PDB 1c5i: Hydrogen Bonding and Catalysis: An Unexpected Explanation For How A Single Amino Acid Substitution Can Change the pH Optimum of A GlycosidaseEnzymatic activity of Hydrogen Bonding and Catalysis: An Unexpected Explanation For How A Single Amino Acid Substitution Can Change the pH Optimum of A Glycosidase
All present enzymatic activity of Hydrogen Bonding and Catalysis: An Unexpected Explanation For How A Single Amino Acid Substitution Can Change the pH Optimum of A Glycosidase:
3.2.1.8; Protein crystallography data
The structure of Hydrogen Bonding and Catalysis: An Unexpected Explanation For How A Single Amino Acid Substitution Can Change the pH Optimum of A Glycosidase, PDB code: 1c5i
was solved by
M.D.Joshi,
G.Sidhu,
I.Pot,
G.D.Brayer,
S.G.Withers,
L.P.Mcintosh,
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 Hydrogen Bonding and Catalysis: An Unexpected Explanation For How A Single Amino Acid Substitution Can Change the pH Optimum of A Glycosidase
(pdb code 1c5i). 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 Hydrogen Bonding and Catalysis: An Unexpected Explanation For How A Single Amino Acid Substitution Can Change the pH Optimum of A Glycosidase, PDB code: 1c5i: Fluorine binding site 1 out of 1 in 1c5iGo back to Fluorine Binding Sites List in 1c5i
Fluorine binding site 1 out
of 1 in the Hydrogen Bonding and Catalysis: An Unexpected Explanation For How A Single Amino Acid Substitution Can Change the pH Optimum of A Glycosidase
Mono view Stereo pair view
Reference:
M.D.Joshi,
G.Sidhu,
I.Pot,
G.D.Brayer,
S.G.Withers,
L.P.Mcintosh.
Hydrogen Bonding and Catalysis: A Novel Explanation For How A Single Amino Acid Substitution Can Change the pH Optimum of A Glycosidase. J.Mol.Biol. V. 299 255 2000.
Page generated: Sun Dec 13 11:28:37 2020
ISSN: ISSN 0022-2836 PubMed: 10860737 DOI: 10.1006/JMBI.2000.3722 |
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