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Atomistry » Zinc » PDB 1jpu-1k51 » 1k4g » |
Zinc in PDB 1k4g: Crystal Structure of Trna-Guanine Transglycosylase (Tgt) Complexed with 2,6-Diamino-8-(1H-Imidazol-2-Ylsulfanylmethyl)-3H-Quinazoline-4- OneEnzymatic activity of Crystal Structure of Trna-Guanine Transglycosylase (Tgt) Complexed with 2,6-Diamino-8-(1H-Imidazol-2-Ylsulfanylmethyl)-3H-Quinazoline-4- One
All present enzymatic activity of Crystal Structure of Trna-Guanine Transglycosylase (Tgt) Complexed with 2,6-Diamino-8-(1H-Imidazol-2-Ylsulfanylmethyl)-3H-Quinazoline-4- One:
2.4.2.29; Protein crystallography data
The structure of Crystal Structure of Trna-Guanine Transglycosylase (Tgt) Complexed with 2,6-Diamino-8-(1H-Imidazol-2-Ylsulfanylmethyl)-3H-Quinazoline-4- One, PDB code: 1k4g
was solved by
R.Brenk,
E.A.Meyer,
R.K.Castellano,
M.Furler,
M.T.Stubbs,
G.Klebe,
F.Diederich,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Zinc Binding Sites:
The binding sites of Zinc atom in the Crystal Structure of Trna-Guanine Transglycosylase (Tgt) Complexed with 2,6-Diamino-8-(1H-Imidazol-2-Ylsulfanylmethyl)-3H-Quinazoline-4- One
(pdb code 1k4g). 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 Crystal Structure of Trna-Guanine Transglycosylase (Tgt) Complexed with 2,6-Diamino-8-(1H-Imidazol-2-Ylsulfanylmethyl)-3H-Quinazoline-4- One, PDB code: 1k4g: Zinc binding site 1 out of 1 in 1k4gGo back to Zinc Binding Sites List in 1k4g
Zinc binding site 1 out
of 1 in the Crystal Structure of Trna-Guanine Transglycosylase (Tgt) Complexed with 2,6-Diamino-8-(1H-Imidazol-2-Ylsulfanylmethyl)-3H-Quinazoline-4- One
Mono view Stereo pair view
Reference:
E.A.Meyer,
R.Brenk,
R.K.Castellano,
M.Furler,
G.Klebe,
F.Diederich.
De Novo Design, Synthesis, and in Vitro Evaluation of Inhibitors For Prokaryotic Trna-Guanine Transglycosylase: A Dramatic Sulfur Effect on Binding Affinity. Chembiochem V. 3 250 2002.
Page generated: Sun Oct 13 04:02:03 2024
ISSN: ISSN 1439-4227 PubMed: 11921407 DOI: 10.1002/1439-7633(20020301)3:2/3<250::AID-CBIC250>3.0.CO;2-J |
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