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Atomistry » Chlorine » PDB 5j7g-5jed » 5j9m | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 5j7g-5jed » 5j9m » |
Chlorine 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:
Chlorine Binding Sites:
The binding sites of Chlorine 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 Chlorine atom.
In total only one binding site of Chlorine was determined in the Trna Guanine Transglycosylase (Tgt) in Co-Crystallized Complex with 2- (Methylamino)-1H-Benzo[D]Imidazole-5-Carboxamide, PDB code: 5j9m: Chlorine binding site 1 out of 1 in 5j9mGo back to![]() ![]()
Chlorine 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: Sat Jul 12 03:29:46 2025
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