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Atomistry » Sodium » PDB 4c6s-4cnt » 4ch2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Sodium » PDB 4c6s-4cnt » 4ch2 » |
Sodium in PDB 4ch2: Low-Salt Crystal Structure of A Thrombin-Gpibalpha Peptide ComplexEnzymatic activity of Low-Salt Crystal Structure of A Thrombin-Gpibalpha Peptide Complex
All present enzymatic activity of Low-Salt Crystal Structure of A Thrombin-Gpibalpha Peptide Complex:
3.4.21.5; Protein crystallography data
The structure of Low-Salt Crystal Structure of A Thrombin-Gpibalpha Peptide Complex, PDB code: 4ch2
was solved by
B.C.Lechtenberg,
S.M.V.Freund,
J.A.Huntington,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Sodium Binding Sites:
The binding sites of Sodium atom in the Low-Salt Crystal Structure of A Thrombin-Gpibalpha Peptide Complex
(pdb code 4ch2). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 2 binding sites of Sodium where determined in the Low-Salt Crystal Structure of A Thrombin-Gpibalpha Peptide Complex, PDB code: 4ch2: Jump to Sodium binding site number: 1; 2; Sodium binding site 1 out of 2 in 4ch2Go back to Sodium Binding Sites List in 4ch2
Sodium binding site 1 out
of 2 in the Low-Salt Crystal Structure of A Thrombin-Gpibalpha Peptide Complex
Mono view Stereo pair view
Sodium binding site 2 out of 2 in 4ch2Go back to Sodium Binding Sites List in 4ch2
Sodium binding site 2 out
of 2 in the Low-Salt Crystal Structure of A Thrombin-Gpibalpha Peptide Complex
Mono view Stereo pair view
Reference:
B.C.Lechtenberg,
S.M.V.Freund,
J.A.Huntington.
Gpibalpha Interacts Exclusively with Exosite II of Thrombin J.Mol.Biol. V. 426 881 2014.
Page generated: Mon Oct 7 14:43:41 2024
ISSN: ISSN 0022-2836 PubMed: 24316004 DOI: 10.1016/J.JMB.2013.11.027 |
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