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Atomistry » Potassium » PDB 1yjn-2aaq » 1yjn » |
Potassium in PDB 1yjn: Crystal Structure of Clindamycin Bound to the G2099A Mutant 50S Ribosomal Subunit of Haloarcula MarismortuiProtein crystallography data
The structure of Crystal Structure of Clindamycin Bound to the G2099A Mutant 50S Ribosomal Subunit of Haloarcula Marismortui, PDB code: 1yjn
was solved by
D.Tu,
G.Blaha,
P.B.Moore,
T.A.Steitz,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 1yjn:
The structure of Crystal Structure of Clindamycin Bound to the G2099A Mutant 50S Ribosomal Subunit of Haloarcula Marismortui also contains other interesting chemical elements:
Potassium Binding Sites:
The binding sites of Potassium atom in the Crystal Structure of Clindamycin Bound to the G2099A Mutant 50S Ribosomal Subunit of Haloarcula Marismortui
(pdb code 1yjn). 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 Clindamycin Bound to the G2099A Mutant 50S Ribosomal Subunit of Haloarcula Marismortui, PDB code: 1yjn: Jump to Potassium binding site number: 1; 2; Potassium binding site 1 out of 2 in 1yjnGo back to Potassium Binding Sites List in 1yjn
Potassium binding site 1 out
of 2 in the Crystal Structure of Clindamycin Bound to the G2099A Mutant 50S Ribosomal Subunit of Haloarcula Marismortui
Mono view Stereo pair view
Potassium binding site 2 out of 2 in 1yjnGo back to Potassium Binding Sites List in 1yjn
Potassium binding site 2 out
of 2 in the Crystal Structure of Clindamycin Bound to the G2099A Mutant 50S Ribosomal Subunit of Haloarcula Marismortui
Mono view Stereo pair view
Reference:
D.Tu,
G.Blaha,
P.B.Moore,
T.A.Steitz.
Structures of Mlsbk Antibiotics Bound to Mutated Large Ribosomal Subunits Provide A Structural Explanation For Resistance. Cell(Cambridge,Mass.) V. 121 257 2005.
Page generated: Mon Aug 12 05:51:44 2024
ISSN: ISSN 0092-8674 PubMed: 15851032 DOI: 10.1016/J.CELL.2005.02.005 |
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