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Atomistry » Zinc » PDB 5jmy-5k0w » 5jt6 » |
Zinc in PDB 5jt6: Trna Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with 2- ((2-Morpholinoethyl)Amino)-1H-Benzo[D]Imidazole-5-CarbohydrazideEnzymatic activity of Trna Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with 2- ((2-Morpholinoethyl)Amino)-1H-Benzo[D]Imidazole-5-Carbohydrazide
All present enzymatic activity of Trna Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with 2- ((2-Morpholinoethyl)Amino)-1H-Benzo[D]Imidazole-5-Carbohydrazide:
2.4.2.29; Protein crystallography data
The structure of Trna Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with 2- ((2-Morpholinoethyl)Amino)-1H-Benzo[D]Imidazole-5-Carbohydrazide, PDB code: 5jt6
was solved by
F.R.Ehrmann,
A.Heine,
G.Klebe,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 5jt6:
The structure of Trna Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with 2- ((2-Morpholinoethyl)Amino)-1H-Benzo[D]Imidazole-5-Carbohydrazide also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Trna Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with 2- ((2-Morpholinoethyl)Amino)-1H-Benzo[D]Imidazole-5-Carbohydrazide
(pdb code 5jt6). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total only one binding site of Zinc was determined in the Trna Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with 2- ((2-Morpholinoethyl)Amino)-1H-Benzo[D]Imidazole-5-Carbohydrazide, PDB code: 5jt6: Zinc binding site 1 out of 1 in 5jt6Go back to Zinc Binding Sites List in 5jt6
Zinc binding site 1 out
of 1 in the Trna Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with 2- ((2-Morpholinoethyl)Amino)-1H-Benzo[D]Imidazole-5-Carbohydrazide
Mono view Stereo pair view
Reference:
F.R.Ehrmann,
C.Hohn,
A.Heine,
F.Diederich,
G.Klebe.
Benzimidazole-Based Inhibitors As A Novel Scaffold to Inhibit Z.Mobilis Tgt and Study Protein Flexibility and the Contributions of Active Site Residues to Binding Affinity of Lin-Benzopurines. To Be Published.
Page generated: Wed Dec 16 06:25:49 2020
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