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Atomistry » Zinc » PDB 6h0w-6h52 » 6h42 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 6h0w-6h52 » 6h42 » |
Zinc in PDB 6h42: Crystal Structure of the Human Tgt Catalytic Subunit QTRT1Enzymatic activity of Crystal Structure of the Human Tgt Catalytic Subunit QTRT1
All present enzymatic activity of Crystal Structure of the Human Tgt Catalytic Subunit QTRT1:
2.4.2.29; Protein crystallography data
The structure of Crystal Structure of the Human Tgt Catalytic Subunit QTRT1, PDB code: 6h42
was solved by
S.Johannsson,
P.Neumann,
R.Ficner,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 6h42:
The structure of Crystal Structure of the Human Tgt Catalytic Subunit QTRT1 also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of the Human Tgt Catalytic Subunit QTRT1
(pdb code 6h42). 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 Human Tgt Catalytic Subunit QTRT1, PDB code: 6h42: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 6h42Go back to![]() ![]()
Zinc binding site 1 out
of 2 in the Crystal Structure of the Human Tgt Catalytic Subunit QTRT1
![]() Mono view ![]() Stereo pair view
Zinc binding site 2 out of 2 in 6h42Go back to![]() ![]()
Zinc binding site 2 out
of 2 in the Crystal Structure of the Human Tgt Catalytic Subunit QTRT1
![]() Mono view ![]() Stereo pair view
Reference:
S.Johannsson,
P.Neumann,
R.Ficner.
Crystal Structure of the Human Trna Guanine Transglycosylase Catalytic Subunit QTRT1. Biomolecules V. 8 2018.
Page generated: Mon Oct 28 22:23:08 2024
ISSN: ISSN 2218-273X PubMed: 30149595 DOI: 10.3390/BIOM8030081 |
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