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Atomistry » Zinc » PDB 5j1q-5jf1 » 5j9m | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 5j1q-5jf1 » 5j9m » |
Zinc in PDB 5j9m: Trna Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with 2- (Methylamino)-1H-Benzo[D]Imidazole-5-CarboxamideEnzymatic activity of Trna Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with 2- (Methylamino)-1H-Benzo[D]Imidazole-5-Carboxamide
All present enzymatic activity of Trna Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with 2- (Methylamino)-1H-Benzo[D]Imidazole-5-Carboxamide:
2.4.2.29; Protein crystallography data
The structure of Trna Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with 2- (Methylamino)-1H-Benzo[D]Imidazole-5-Carboxamide, PDB code: 5j9m
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 5j9m:
The structure of Trna Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with 2- (Methylamino)-1H-Benzo[D]Imidazole-5-Carboxamide 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- (Methylamino)-1H-Benzo[D]Imidazole-5-Carboxamide
(pdb code 5j9m). 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- (Methylamino)-1H-Benzo[D]Imidazole-5-Carboxamide, PDB code: 5j9m: Zinc binding site 1 out of 1 in 5j9mGo back to![]() ![]()
Zinc binding site 1 out
of 1 in the Trna Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with 2- (Methylamino)-1H-Benzo[D]Imidazole-5-Carboxamide
![]() 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: Sun Oct 27 18:42:15 2024
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