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Atomistry » Chlorine » PDB 5o5t-5oeh » 5oc5 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Chlorine » PDB 5o5t-5oeh » 5oc5 » |
Chlorine in PDB 5oc5: Crystal Structure of Human Trna-Dihydrouridine(20) Synthase Dsrbd K419A-K420A MutantProtein crystallography data
The structure of Crystal Structure of Human Trna-Dihydrouridine(20) Synthase Dsrbd K419A-K420A Mutant, PDB code: 5oc5
was solved by
C.Bou-Nader,
L.Pecqueur,
D.Hamdane,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Chlorine Binding Sites:
The binding sites of Chlorine atom in the Crystal Structure of Human Trna-Dihydrouridine(20) Synthase Dsrbd K419A-K420A Mutant
(pdb code 5oc5). This binding sites where shown within
5.0 Angstroms radius around Chlorine atom.
In total 2 binding sites of Chlorine where determined in the Crystal Structure of Human Trna-Dihydrouridine(20) Synthase Dsrbd K419A-K420A Mutant, PDB code: 5oc5: Jump to Chlorine binding site number: 1; 2; Chlorine binding site 1 out of 2 in 5oc5Go back to Chlorine Binding Sites List in 5oc5
Chlorine binding site 1 out
of 2 in the Crystal Structure of Human Trna-Dihydrouridine(20) Synthase Dsrbd K419A-K420A Mutant
Mono view Stereo pair view
Chlorine binding site 2 out of 2 in 5oc5Go back to Chlorine Binding Sites List in 5oc5
Chlorine binding site 2 out
of 2 in the Crystal Structure of Human Trna-Dihydrouridine(20) Synthase Dsrbd K419A-K420A Mutant
Mono view Stereo pair view
Reference:
C.Bou-Nader,
P.Barraud,
L.Pecqueur,
J.Perez,
C.Velours,
W.Shepard,
M.Fontecave,
C.Tisne,
D.Hamdane.
Molecular Basis For Transfer Rna Recognition By the Double-Stranded Rna-Binding Domain of Human Dihydrouridine Synthase 2. Nucleic Acids Res. V. 47 3117 2019.
Page generated: Fri Jul 26 14:23:57 2024
ISSN: ESSN 1362-4962 PubMed: 30605527 DOI: 10.1093/NAR/GKY1302 |
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