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Atomistry » Chlorine » PDB 2vg2-2vo5 » 2vj0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 2vg2-2vo5 » 2vj0 » |
Chlorine in PDB 2vj0: Crystal Structure of the Alpha-Adaptin Appendage Domain, From the AP2 Adaptor Complex, in Complex with An Fxdnf Peptide From AMPHIPHYSIN1 and A Wvxf Peptide From Synaptojanin P170Protein crystallography data
The structure of Crystal Structure of the Alpha-Adaptin Appendage Domain, From the AP2 Adaptor Complex, in Complex with An Fxdnf Peptide From AMPHIPHYSIN1 and A Wvxf Peptide From Synaptojanin P170, PDB code: 2vj0
was solved by
M.G.J.Ford,
G.J.K.Praefcke,
H.T.Mcmahon,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of the Alpha-Adaptin Appendage Domain, From the AP2 Adaptor Complex, in Complex with An Fxdnf Peptide From AMPHIPHYSIN1 and A Wvxf Peptide From Synaptojanin P170
(pdb code 2vj0). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total only one binding site of Chlorine was determined in the Crystal Structure of the Alpha-Adaptin Appendage Domain, From the AP2 Adaptor Complex, in Complex with An Fxdnf Peptide From AMPHIPHYSIN1 and A Wvxf Peptide From Synaptojanin P170, PDB code: 2vj0: Chlorine binding site 1 out of 1 in 2vj0Go back to![]() ![]()
Chlorine binding site 1 out
of 1 in the Crystal Structure of the Alpha-Adaptin Appendage Domain, From the AP2 Adaptor Complex, in Complex with An Fxdnf Peptide From AMPHIPHYSIN1 and A Wvxf Peptide From Synaptojanin P170
![]() Mono view ![]() Stereo pair view
Reference:
L.E.Olesen,
M.G.J.Ford,
E.M.Schmid,
Y.Vallis,
M.Madan Babu,
P.H.Li,
I.G.Mills,
H.T.Mcmahon,
G.J.K.Praefcke.
Solitary and Repetitive Binding Motifs For the AP2 Complex {Alpha}-Appendage in Amphiphysin and Other Accessory Proteins. J.Biol.Chem. V. 283 5099 2008.
Page generated: Sat Jul 20 11:54:13 2024
ISSN: ISSN 0021-9258 PubMed: 17986441 DOI: 10.1074/JBC.M708621200 |
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