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Atomistry » Mercury » PDB 1yu1-2epm » 2byt » |
Mercury in PDB 2byt: Thermus Thermophilus Leucyl-Trna Synthetase Complexed with A Trnaleu Transcript in the Post-Editing ConformationProtein crystallography data
The structure of Thermus Thermophilus Leucyl-Trna Synthetase Complexed with A Trnaleu Transcript in the Post-Editing Conformation, PDB code: 2byt
was solved by
S.Cusack,
M.Tukalo,
A.Yaremchuk,
R.Fukunaga,
S.Yokoyama,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 2byt:
The structure of Thermus Thermophilus Leucyl-Trna Synthetase Complexed with A Trnaleu Transcript in the Post-Editing Conformation also contains other interesting chemical elements:
Mercury Binding Sites:
The binding sites of Mercury atom in the Thermus Thermophilus Leucyl-Trna Synthetase Complexed with A Trnaleu Transcript in the Post-Editing Conformation
(pdb code 2byt). This binding sites where shown within
5.0 Angstroms radius around Mercury atom.
In total 2 binding sites of Mercury where determined in the Thermus Thermophilus Leucyl-Trna Synthetase Complexed with A Trnaleu Transcript in the Post-Editing Conformation, PDB code: 2byt: Jump to Mercury binding site number: 1; 2; Mercury binding site 1 out of 2 in 2bytGo back to Mercury Binding Sites List in 2byt
Mercury binding site 1 out
of 2 in the Thermus Thermophilus Leucyl-Trna Synthetase Complexed with A Trnaleu Transcript in the Post-Editing Conformation
Mono view Stereo pair view
Mercury binding site 2 out of 2 in 2bytGo back to Mercury Binding Sites List in 2byt
Mercury binding site 2 out
of 2 in the Thermus Thermophilus Leucyl-Trna Synthetase Complexed with A Trnaleu Transcript in the Post-Editing Conformation
Mono view Stereo pair view
Reference:
M.Tukalo,
A.Yaremchuk,
R.Fukunaga,
S.Yokoyama,
S.Cusack.
The Crystal Structure of Leucyl-Trna Synthetase Complexed with Trna(Leu) in the Post-Transfer- Editing Conformation. Nat.Struct.Mol.Biol. V. 12 923 2005.
Page generated: Sun Aug 11 02:21:06 2024
ISSN: ISSN 1545-9993 PubMed: 16155583 DOI: 10.1038/NSMB986 |
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