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Atomistry » Zinc » PDB 5b3s-5brv » 5b4e | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 5b3s-5brv » 5b4e » |
Zinc in PDB 5b4e: Sulfur Transferase Ttua in Complex with Iron Sulfur Cluster and Atp DerivativeProtein crystallography data
The structure of Sulfur Transferase Ttua in Complex with Iron Sulfur Cluster and Atp Derivative, PDB code: 5b4e
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 5b4e:
The structure of Sulfur Transferase Ttua in Complex with Iron Sulfur Cluster and Atp Derivative 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 and Atp Derivative
(pdb code 5b4e). 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 and Atp Derivative, PDB code: 5b4e: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 5b4eGo back to![]() ![]()
Zinc binding site 1 out
of 2 in the Sulfur Transferase Ttua in Complex with Iron Sulfur Cluster and Atp Derivative
![]() Mono view ![]() Stereo pair view
Zinc binding site 2 out of 2 in 5b4eGo back to![]() ![]()
Zinc binding site 2 out
of 2 in the Sulfur Transferase Ttua in Complex with Iron Sulfur Cluster and Atp Derivative
![]() 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: Thu Aug 21 00:54:23 2025
ISSN: ESSN 1091-6490 PubMed: 28439027 DOI: 10.1073/PNAS.1615585114 |
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