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Atomistry » Zinc » PDB 1ed8-1evl » 1efz » |
Zinc in PDB 1efz: Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic ActivityEnzymatic activity of Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity
All present enzymatic activity of Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity:
2.4.2.29; Protein crystallography data
The structure of Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity, PDB code: 1efz
was solved by
U.Gradler,
R.Ficner,
G.A.Garcia,
M.T.Stubbs,
G.Klebe,
K.Reuter,
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 Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity
(pdb code 1efz). 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 Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity, PDB code: 1efz: Zinc binding site 1 out of 1 in 1efzGo back to Zinc Binding Sites List in 1efz
Zinc binding site 1 out
of 1 in the Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna- Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity
Mono view Stereo pair view
Reference:
U.Gradler,
R.Ficner,
G.A.Garcia,
M.T.Stubbs,
G.Klebe,
K.Reuter.
Mutagenesis and Crystallographic Studies of Zymomonas Mobilis Trna-Guanine Transglycosylase to Elucidate the Role of Serine 103 For Enzymatic Activity. Febs Lett. V. 454 142 1999.
Page generated: Sun Oct 13 00:13:21 2024
ISSN: ISSN 0014-5793 PubMed: 10413112 DOI: 10.1016/S0014-5793(99)00793-0 |
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