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Atomistry » Sodium » PDB 5vxa-5wiv » 5w6s | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 5vxa-5wiv » 5w6s » |
Sodium in PDB 5w6s: Crystal Structure of Bacteriophage CBA120 Tailspike Protein 2 Enzymatically Active Domain (TSP2DN, ORF211) Complex with Escherichia Coli O157-AntigenProtein crystallography data
The structure of Crystal Structure of Bacteriophage CBA120 Tailspike Protein 2 Enzymatically Active Domain (TSP2DN, ORF211) Complex with Escherichia Coli O157-Antigen, PDB code: 5w6s
was solved by
M.Plattner,
M.M.Shneider,
P.G.Leiman,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5w6s:
The structure of Crystal Structure of Bacteriophage CBA120 Tailspike Protein 2 Enzymatically Active Domain (TSP2DN, ORF211) Complex with Escherichia Coli O157-Antigen also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of Bacteriophage CBA120 Tailspike Protein 2 Enzymatically Active Domain (TSP2DN, ORF211) Complex with Escherichia Coli O157-Antigen
(pdb code 5w6s). 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 Bacteriophage CBA120 Tailspike Protein 2 Enzymatically Active Domain (TSP2DN, ORF211) Complex with Escherichia Coli O157-Antigen, PDB code: 5w6s: Sodium binding site 1 out of 1 in 5w6sGo back to Sodium Binding Sites List in 5w6s
Sodium binding site 1 out
of 1 in the Crystal Structure of Bacteriophage CBA120 Tailspike Protein 2 Enzymatically Active Domain (TSP2DN, ORF211) Complex with Escherichia Coli O157-Antigen
Mono view Stereo pair view
Reference:
M.Plattner,
M.M.Shneider,
N.P.Arbatsky,
A.S.Shashkov,
A.O.Chizhov,
S.Nazarov,
N.S.Prokhorov,
N.M.I.Taylor,
S.A.Buth,
M.Gambino,
Y.E.Gencay,
L.Brondsted,
E.M.Kutter,
Y.A.Knirel,
P.G.Leiman.
Structure and Function of the Branched Receptor-Binding Complex of Bacteriophage CBA120. J.Mol.Biol. V. 431 3718 2019.
Page generated: Tue Dec 15 11:47:16 2020
ISSN: ESSN 1089-8638 PubMed: 31325442 DOI: 10.1016/J.JMB.2019.07.022 |
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