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Atomistry » Magnesium » PDB 3q89-3qpo » 3qo8 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Magnesium » PDB 3q89-3qpo » 3qo8 » |
Magnesium in PDB 3qo8: Crystal Structure of Seryl-Trna Synthetase From Candida AlbicansEnzymatic activity of Crystal Structure of Seryl-Trna Synthetase From Candida Albicans
All present enzymatic activity of Crystal Structure of Seryl-Trna Synthetase From Candida Albicans:
6.1.1.11; Protein crystallography data
The structure of Crystal Structure of Seryl-Trna Synthetase From Candida Albicans, PDB code: 3qo8
was solved by
R.Rocha,
M.A.Santos,
P.J.B.Pereira,
S.Macedo-Ribeiro,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Magnesium Binding Sites:
The binding sites of Magnesium atom in the Crystal Structure of Seryl-Trna Synthetase From Candida Albicans
(pdb code 3qo8). This binding sites where shown within
5.0 Angstroms radius around Magnesium atom.
In total 2 binding sites of Magnesium where determined in the Crystal Structure of Seryl-Trna Synthetase From Candida Albicans, PDB code: 3qo8: Jump to Magnesium binding site number: 1; 2; Magnesium binding site 1 out of 2 in 3qo8Go back to Magnesium Binding Sites List in 3qo8
Magnesium binding site 1 out
of 2 in the Crystal Structure of Seryl-Trna Synthetase From Candida Albicans
Mono view Stereo pair view
Magnesium binding site 2 out of 2 in 3qo8Go back to Magnesium Binding Sites List in 3qo8
Magnesium binding site 2 out
of 2 in the Crystal Structure of Seryl-Trna Synthetase From Candida Albicans
Mono view Stereo pair view
Reference:
R.Rocha,
P.J.Pereira,
M.A.Santos,
S.Macedo-Ribeiro.
Unveiling the Structural Basis For Translational Ambiguity Tolerance in A Human Fungal Pathogen. Proc.Natl.Acad.Sci.Usa V. 108 14091 2011.
Page generated: Thu Aug 15 10:06:01 2024
ISSN: ISSN 0027-8424 PubMed: 21825144 DOI: 10.1073/PNAS.1102835108 |
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