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Atomistry » Potassium » PDB 2xo1-3atv » 2ycb » |
Potassium in PDB 2ycb: Structure of the Archaeal Beta-Casp Protein with N-Terminal Kh Domains From Methanothermobacter ThermautotrophicusProtein crystallography data
The structure of Structure of the Archaeal Beta-Casp Protein with N-Terminal Kh Domains From Methanothermobacter Thermautotrophicus, PDB code: 2ycb
was solved by
A.P.G.Silva,
M.Chechik,
R.T.Byrne,
D.G.Waterman,
C.L.Ng,
E.J.Dodson,
E.V.Koonin,
A.A.Antson,
C.Smits,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2ycb:
The structure of Structure of the Archaeal Beta-Casp Protein with N-Terminal Kh Domains From Methanothermobacter Thermautotrophicus also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Structure of the Archaeal Beta-Casp Protein with N-Terminal Kh Domains From Methanothermobacter Thermautotrophicus
(pdb code 2ycb). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Structure of the Archaeal Beta-Casp Protein with N-Terminal Kh Domains From Methanothermobacter Thermautotrophicus, PDB code: 2ycb: Jump to Potassium binding site number: 1; 2; Potassium binding site 1 out of 2 in 2ycbGo back to![]() ![]()
Potassium binding site 1 out
of 2 in the Structure of the Archaeal Beta-Casp Protein with N-Terminal Kh Domains From Methanothermobacter Thermautotrophicus
![]() Mono view ![]() Stereo pair view
Potassium binding site 2 out of 2 in 2ycbGo back to![]() ![]()
Potassium binding site 2 out
of 2 in the Structure of the Archaeal Beta-Casp Protein with N-Terminal Kh Domains From Methanothermobacter Thermautotrophicus
![]() Mono view ![]() Stereo pair view
Reference:
A.P.G.Silva,
M.Chechik,
R.T.Byrne,
D.G.Waterman,
C.L.Ng,
E.J.Dodson,
E.V.Koonin,
A.A.Antson,
C.Smits.
Structure and Activity of A Novel Archaeal Beta-Casp Protein with N-Terminal Kh Domains. Structure V. 19 622 2011.
Page generated: Sat Aug 9 04:26:22 2025
ISSN: ISSN 0969-2126 PubMed: 21565697 DOI: 10.1016/J.STR.2011.03.002 |
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