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Atomistry » Zinc » PDB 2zep-2zxg » 2ztg » |
Zinc in PDB 2ztg: Crystal Structure of Archaeoglobus Fulgidus Alanyl-Trna Synthetase Lacking the C-Terminal Dimerization Domain in Complex with Ala-SaEnzymatic activity of Crystal Structure of Archaeoglobus Fulgidus Alanyl-Trna Synthetase Lacking the C-Terminal Dimerization Domain in Complex with Ala-Sa
All present enzymatic activity of Crystal Structure of Archaeoglobus Fulgidus Alanyl-Trna Synthetase Lacking the C-Terminal Dimerization Domain in Complex with Ala-Sa:
6.1.1.7; Protein crystallography data
The structure of Crystal Structure of Archaeoglobus Fulgidus Alanyl-Trna Synthetase Lacking the C-Terminal Dimerization Domain in Complex with Ala-Sa, PDB code: 2ztg
was solved by
M.Naganuma,
S.Sekine,
R.Fukunaga,
S.Yokoyama,
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 Archaeoglobus Fulgidus Alanyl-Trna Synthetase Lacking the C-Terminal Dimerization Domain in Complex with Ala-Sa
(pdb code 2ztg). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Crystal Structure of Archaeoglobus Fulgidus Alanyl-Trna Synthetase Lacking the C-Terminal Dimerization Domain in Complex with Ala-Sa, PDB code: 2ztg: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 2ztgGo back to![]() ![]()
Zinc binding site 1 out
of 2 in the Crystal Structure of Archaeoglobus Fulgidus Alanyl-Trna Synthetase Lacking the C-Terminal Dimerization Domain in Complex with Ala-Sa
![]() Mono view ![]() Stereo pair view
Zinc binding site 2 out of 2 in 2ztgGo back to![]() ![]()
Zinc binding site 2 out
of 2 in the Crystal Structure of Archaeoglobus Fulgidus Alanyl-Trna Synthetase Lacking the C-Terminal Dimerization Domain in Complex with Ala-Sa
![]() Mono view ![]() Stereo pair view
Reference:
M.Naganuma,
S.Sekine,
R.Fukunaga,
S.Yokoyama.
Unique Protein Architecture of Alanyl-Trna Synthetase For Aminoacylation, Editing, and Dimerization. Proc.Natl.Acad.Sci.Usa V. 106 8489 2009.
Page generated: Thu Oct 24 10:53:17 2024
ISSN: ISSN 0027-8424 PubMed: 19423669 DOI: 10.1073/PNAS.0901572106 |
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