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Atomistry » Sodium » PDB 3vif-3way » 3vw7 » |
Sodium 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:
Sodium Binding Sites:
The binding sites of Sodium 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 Sodium atom.
In total only one binding site of Sodium was determined in the Crystal Structure of Human Protease-Activated Receptor 1 (PAR1) Bound with Antagonist Vorapaxar at 2.2 Angstrom, PDB code: 3vw7: Sodium binding site 1 out of 1 in 3vw7Go back to![]() ![]()
Sodium 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: Mon Oct 7 13:52:26 2024
ISSN: ISSN 0028-0836 PubMed: 23222541 DOI: 10.1038/NATURE11701 |
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