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Atomistry » Zinc » PDB 5b2q-5brk » 5b4f | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 5b2q-5brk » 5b4f » |
Zinc in PDB 5b4f: Sulfur Transferase Ttua in Complex with Iron Sulfur ClusterProtein crystallography data
The structure of Sulfur Transferase Ttua in Complex with Iron Sulfur Cluster, PDB code: 5b4f
was solved by
M.Chen,
S.Narai,
Y.Tanaka,
M.Yao,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5b4f:
The structure of Sulfur Transferase Ttua in Complex with Iron Sulfur Cluster also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Sulfur Transferase Ttua in Complex with Iron Sulfur Cluster
(pdb code 5b4f). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Sulfur Transferase Ttua in Complex with Iron Sulfur Cluster, PDB code: 5b4f: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 5b4fGo back to Zinc Binding Sites List in 5b4f
Zinc binding site 1 out
of 2 in the Sulfur Transferase Ttua in Complex with Iron Sulfur Cluster
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 5b4fGo back to Zinc Binding Sites List in 5b4f
Zinc binding site 2 out
of 2 in the Sulfur Transferase Ttua in Complex with Iron Sulfur Cluster
Mono view Stereo pair view
Reference:
M.Chen,
S.I.Asai,
S.Narai,
S.Nambu,
N.Omura,
Y.Sakaguchi,
T.Suzuki,
M.Ikeda-Saito,
K.Watanabe,
M.Yao,
N.Shigi,
Y.Tanaka.
Biochemical and Structural Characterization of Oxygen-Sensitive 2-Thiouridine Synthesis Catalyzed By An Iron-Sulfur Protein Ttua Proc. Natl. Acad. Sci. V. 114 4954 2017U.S.A..
Page generated: Wed Dec 16 06:04:31 2020
ISSN: ESSN 1091-6490 PubMed: 28439027 DOI: 10.1073/PNAS.1615585114 |
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