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Atomistry » Potassium » PDB 2o8l-2qxl » 2pa2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Potassium » PDB 2o8l-2qxl » 2pa2 » |
Potassium in PDB 2pa2: Crystal Structure of Human Ribosomal Protein L10 Core DomainProtein crystallography data
The structure of Crystal Structure of Human Ribosomal Protein L10 Core Domain, PDB code: 2pa2
was solved by
M.Nishimura,
T.Kaminishi,
C.Takemoto,
M.Kawazoe,
T.Yoshida,
A.Tanaka,
S.Sugano,
M.Shirouzu,
T.Ohkubo,
S.Yokoyama,
Y.Kobayashi,
Riken Structuralgenomics/Proteomics Initiative (Rsgi),
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Potassium Binding Sites:
The binding sites of Potassium atom in the Crystal Structure of Human Ribosomal Protein L10 Core Domain
(pdb code 2pa2). This binding sites where shown within
5.0 Angstroms radius around Potassium atom.
In total 2 binding sites of Potassium where determined in the Crystal Structure of Human Ribosomal Protein L10 Core Domain, PDB code: 2pa2: Jump to Potassium binding site number: 1; 2; Potassium binding site 1 out of 2 in 2pa2Go back to Potassium Binding Sites List in 2pa2
Potassium binding site 1 out
of 2 in the Crystal Structure of Human Ribosomal Protein L10 Core Domain
Mono view Stereo pair view
Potassium binding site 2 out of 2 in 2pa2Go back to Potassium Binding Sites List in 2pa2
Potassium binding site 2 out
of 2 in the Crystal Structure of Human Ribosomal Protein L10 Core Domain
Mono view Stereo pair view
Reference:
M.Nishimura,
T.Kaminishi,
C.Takemoto,
M.Kawazoe,
T.Yoshida,
A.Tanaka,
S.Sugano,
M.Shirouzu,
T.Ohkubo,
S.Yokoyama,
Y.Kobayashi.
Crystal Structure of Human Ribosomal Protein L10 Core Domain Reveals Eukaryote-Specific Motifs in Addition to the Conserved Fold J.Mol.Biol. V. 377 421 2008.
Page generated: Mon Aug 12 06:50:58 2024
ISSN: ISSN 0022-2836 PubMed: 18258260 DOI: 10.1016/J.JMB.2008.01.003 |
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