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Atomistry » Zinc » PDB 4d91-4dr2 » 4dr2 » |
Zinc in PDB 4dr2: Crystal Structure of the Thermus Thermophilus (HB8) 30S Ribosomal Subunit with Multiple Copies of Paromomycin Molecules BoundProtein crystallography data
The structure of Crystal Structure of the Thermus Thermophilus (HB8) 30S Ribosomal Subunit with Multiple Copies of Paromomycin Molecules Bound, PDB code: 4dr2
was solved by
H.Demirci,
F.Murphy Iv,
E.Murphy,
S.T.Gregory,
A.E.Dahlberg,
G.Jogl,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4dr2:
The structure of Crystal Structure of the Thermus Thermophilus (HB8) 30S Ribosomal Subunit with Multiple Copies of Paromomycin Molecules Bound also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of the Thermus Thermophilus (HB8) 30S Ribosomal Subunit with Multiple Copies of Paromomycin Molecules Bound
(pdb code 4dr2). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of the Thermus Thermophilus (HB8) 30S Ribosomal Subunit with Multiple Copies of Paromomycin Molecules Bound, PDB code: 4dr2: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 4dr2Go back to Zinc Binding Sites List in 4dr2
Zinc binding site 1 out
of 2 in the Crystal Structure of the Thermus Thermophilus (HB8) 30S Ribosomal Subunit with Multiple Copies of Paromomycin Molecules Bound
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 4dr2Go back to Zinc Binding Sites List in 4dr2
Zinc binding site 2 out
of 2 in the Crystal Structure of the Thermus Thermophilus (HB8) 30S Ribosomal Subunit with Multiple Copies of Paromomycin Molecules Bound
Mono view Stereo pair view
Reference:
H.Demirci,
F.Murphy,
E.Murphy,
S.T.Gregory,
A.E.Dahlberg,
G.Jogl.
A Structural Basis For Streptomycin-Induced Misreading of the Genetic Code. Nat Commun V. 4 1355 2013.
Page generated: Sat Oct 26 21:33:59 2024
ISSN: ESSN 2041-1723 PubMed: 23322043 DOI: 10.1038/NCOMMS2346 |
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