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Atomistry » Sodium » PDB 2ply-2qd6 » 2pmh » |
Sodium in PDB 2pmh: Crystal Structure of THR132ALA of ST1022 From Sulfolobus TokodaiiProtein crystallography data
The structure of Crystal Structure of THR132ALA of ST1022 From Sulfolobus Tokodaii, PDB code: 2pmh
was solved by
T.S.Kumarevel,
P.Karthe,
N.Nakano,
A.Shinkai,
S.Yokoyama,
Riken Structuralgenomics/Proteomics Initiative (Rsgi),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2pmh:
The structure of Crystal Structure of THR132ALA of ST1022 From Sulfolobus Tokodaii also contains other interesting chemical elements:
Sodium Binding Sites:
The binding sites of Sodium atom in the Crystal Structure of THR132ALA of ST1022 From Sulfolobus Tokodaii
(pdb code 2pmh). This binding sites where shown within
5.0 Angstroms radius around Sodium atom.
In total 3 binding sites of Sodium where determined in the Crystal Structure of THR132ALA of ST1022 From Sulfolobus Tokodaii, PDB code: 2pmh: Jump to Sodium binding site number: 1; 2; 3; Sodium binding site 1 out of 3 in 2pmhGo back to
Sodium binding site 1 out
of 3 in the Crystal Structure of THR132ALA of ST1022 From Sulfolobus Tokodaii
![]() Mono view ![]() Stereo pair view
Sodium binding site 2 out of 3 in 2pmhGo back to
Sodium binding site 2 out
of 3 in the Crystal Structure of THR132ALA of ST1022 From Sulfolobus Tokodaii
![]() Mono view ![]() Stereo pair view
Sodium binding site 3 out of 3 in 2pmhGo back to
Sodium binding site 3 out
of 3 in the Crystal Structure of THR132ALA of ST1022 From Sulfolobus Tokodaii
![]() Mono view ![]() Stereo pair view
Reference:
T.S.Kumarevel,
N.Nakano,
K.Ponnuraj,
S.C.B.Gopinath,
K.Sakamoto,
A.Shinkai,
P.K.R.Kumar,
S.Yokoyama.
Crystal Structure of Glutamine Receptor Protein From Sulfolobus Tokodaii Strain 7 in Complex with Its Effector L-Glutamine: Implications of Effector Binding in Molecular Association and Dna Binding Nucleic Acids Res. V. 36 4808 2008.
Page generated: Sun Aug 17 11:21:07 2025
ISSN: ISSN 0305-1048 PubMed: 18653535 DOI: 10.1093/NAR/GKN456 |
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