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Atomistry » Fluorine » PDB 1fko-1h1d » 1fuy » |
Fluorine in PDB 1fuy: Crystal Structure of BETAA169L/BETAC170W Double Mutant of Tryptophan Synthase Complexed with 5-Fluoro-Indole-Propanol PhosphateEnzymatic activity of Crystal Structure of BETAA169L/BETAC170W Double Mutant of Tryptophan Synthase Complexed with 5-Fluoro-Indole-Propanol Phosphate
All present enzymatic activity of Crystal Structure of BETAA169L/BETAC170W Double Mutant of Tryptophan Synthase Complexed with 5-Fluoro-Indole-Propanol Phosphate:
4.2.1.20; Protein crystallography data
The structure of Crystal Structure of BETAA169L/BETAC170W Double Mutant of Tryptophan Synthase Complexed with 5-Fluoro-Indole-Propanol Phosphate, PDB code: 1fuy
was solved by
M.Weyand,
I.Schlichting,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1fuy:
The structure of Crystal Structure of BETAA169L/BETAC170W Double Mutant of Tryptophan Synthase Complexed with 5-Fluoro-Indole-Propanol Phosphate also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of BETAA169L/BETAC170W Double Mutant of Tryptophan Synthase Complexed with 5-Fluoro-Indole-Propanol Phosphate
(pdb code 1fuy). 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 Crystal Structure of BETAA169L/BETAC170W Double Mutant of Tryptophan Synthase Complexed with 5-Fluoro-Indole-Propanol Phosphate, PDB code: 1fuy: Fluorine binding site 1 out of 1 in 1fuyGo back to Fluorine Binding Sites List in 1fuy
Fluorine binding site 1 out
of 1 in the Crystal Structure of BETAA169L/BETAC170W Double Mutant of Tryptophan Synthase Complexed with 5-Fluoro-Indole-Propanol Phosphate
Mono view Stereo pair view
Reference:
M.Weyand,
I.Schlichting.
Structural Basis For the Impaired Channeling and Allosteric Inter-Subunit Communication in the Beta A169L/Beta C170W Mutant of Tryptophan Synthase. J.Biol.Chem. V. 275 41058 2000.
Page generated: Sun Dec 13 11:29:36 2020
ISSN: ISSN 0021-9258 PubMed: 11034989 DOI: 10.1074/JBC.C000479200 |
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