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Atomistry » Fluorine » PDB 3vrs-3wyk » 3vw7 » |
Fluorine in PDB 3vw7: Crystal Structure of Human Protease-Activated Receptor 1 (PAR1) Bound with Antagonist Vorapaxar at 2.2 AngstromEnzymatic activity of Crystal Structure of Human Protease-Activated Receptor 1 (PAR1) Bound with Antagonist Vorapaxar at 2.2 Angstrom
All present enzymatic activity of Crystal Structure of Human Protease-Activated Receptor 1 (PAR1) Bound with Antagonist Vorapaxar at 2.2 Angstrom:
3.2.1.17; Protein crystallography data
The structure of Crystal Structure of Human Protease-Activated Receptor 1 (PAR1) Bound with Antagonist Vorapaxar at 2.2 Angstrom, PDB code: 3vw7
was solved by
C.Zhang,
Y.Srinivasan,
D.H.Arlow,
J.J.Fung,
D.Palmer,
Y.Zheng,
H.F.Green,
A.Pandey,
R.O.Dror,
D.E.Shaw,
W.I.Weis,
S.R.Coughlin,
B.K.Kobilka,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 3vw7:
The structure of Crystal Structure of Human Protease-Activated Receptor 1 (PAR1) Bound with Antagonist Vorapaxar at 2.2 Angstrom also contains other interesting chemical elements:
Fluorine Binding Sites:
The binding sites of Fluorine atom in the Crystal Structure of Human Protease-Activated Receptor 1 (PAR1) Bound with Antagonist Vorapaxar at 2.2 Angstrom
(pdb code 3vw7). 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 Human Protease-Activated Receptor 1 (PAR1) Bound with Antagonist Vorapaxar at 2.2 Angstrom, PDB code: 3vw7: Fluorine binding site 1 out of 1 in 3vw7Go back to Fluorine Binding Sites List in 3vw7
Fluorine binding site 1 out
of 1 in the Crystal Structure of Human Protease-Activated Receptor 1 (PAR1) Bound with Antagonist Vorapaxar at 2.2 Angstrom
Mono view Stereo pair view
Reference:
C.Zhang,
Y.Srinivasan,
D.H.Arlow,
J.J.Fung,
D.Palmer,
Y.Zheng,
H.F.Green,
A.Pandey,
R.O.Dror,
D.E.Shaw,
W.I.Weis,
S.R.Coughlin,
B.K.Kobilka.
High-Resolution Crystal Structure of Human Protease-Activated Receptor 1 Nature V. 492 387 2012.
Page generated: Sun Dec 13 11:57:22 2020
ISSN: ISSN 0028-0836 PubMed: 23222541 DOI: 10.1038/NATURE11701 |
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