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Atomistry » Barium » PDB 5wky-7awm » 5wu2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Barium » PDB 5wky-7awm » 5wu2 » |
Barium in PDB 5wu2: Crystal Structure of Human TUT1 Bound with Bautp, Form IEnzymatic activity of Crystal Structure of Human TUT1 Bound with Bautp, Form I
All present enzymatic activity of Crystal Structure of Human TUT1 Bound with Bautp, Form I:
2.7.7.19; 2.7.7.52; Protein crystallography data
The structure of Crystal Structure of Human TUT1 Bound with Bautp, Form I, PDB code: 5wu2
was solved by
S.Yamashita,
K.Tomita,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5wu2:
The structure of Crystal Structure of Human TUT1 Bound with Bautp, Form I also contains other interesting chemical elements:
Barium Binding Sites:
The binding sites of Barium atom in the Crystal Structure of Human TUT1 Bound with Bautp, Form I
(pdb code 5wu2). This binding sites where shown within
5.0 Angstroms radius around Barium atom.
In total 2 binding sites of Barium where determined in the Crystal Structure of Human TUT1 Bound with Bautp, Form I, PDB code: 5wu2: Jump to Barium binding site number: 1; 2; Barium binding site 1 out of 2 in 5wu2Go back to Barium Binding Sites List in 5wu2
Barium binding site 1 out
of 2 in the Crystal Structure of Human TUT1 Bound with Bautp, Form I
Mono view Stereo pair view
Barium binding site 2 out of 2 in 5wu2Go back to Barium Binding Sites List in 5wu2
Barium binding site 2 out
of 2 in the Crystal Structure of Human TUT1 Bound with Bautp, Form I
Mono view Stereo pair view
Reference:
S.Yamashita,
Y.Takagi,
T.Nagaike,
K.Tomita.
Crystal Structures of U6 Snrna-Specific Terminal Uridylyltransferase Nat Commun V. 8 15788 2017.
Page generated: Wed Jul 10 15:53:50 2024
ISSN: ESSN 2041-1723 PubMed: 28589955 DOI: 10.1038/NCOMMS15788 |
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