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Atomistry » Zinc » PDB 6fgs-6frz » 6fhg » |
Zinc in PDB 6fhg: Crystal Structure of the TS2631 Endolysin From Thermus Scotoductus Phage with the Unique N-Terminal Moiety Responsible For Peptidoglycan AnchoringProtein crystallography data
The structure of Crystal Structure of the TS2631 Endolysin From Thermus Scotoductus Phage with the Unique N-Terminal Moiety Responsible For Peptidoglycan Anchoring, PDB code: 6fhg
was solved by
K.Zeth,
E.Sancho-Vaello,
M.Plotka,
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 the TS2631 Endolysin From Thermus Scotoductus Phage with the Unique N-Terminal Moiety Responsible For Peptidoglycan Anchoring
(pdb code 6fhg). 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 the TS2631 Endolysin From Thermus Scotoductus Phage with the Unique N-Terminal Moiety Responsible For Peptidoglycan Anchoring, PDB code: 6fhg: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 6fhgGo back to Zinc Binding Sites List in 6fhg
Zinc binding site 1 out
of 2 in the Crystal Structure of the TS2631 Endolysin From Thermus Scotoductus Phage with the Unique N-Terminal Moiety Responsible For Peptidoglycan Anchoring
Mono view Stereo pair view
Zinc binding site 2 out of 2 in 6fhgGo back to Zinc Binding Sites List in 6fhg
Zinc binding site 2 out
of 2 in the Crystal Structure of the TS2631 Endolysin From Thermus Scotoductus Phage with the Unique N-Terminal Moiety Responsible For Peptidoglycan Anchoring
Mono view Stereo pair view
Reference:
M.Plotka,
E.Sancho-Vaello,
S.Dorawa,
A.K.Kaczorowska,
L.P.Kozlowski,
T.Kaczorowski,
K.Zeth.
Structure and Function of the TS2631 Endolysin of Thermus Scotoductus Phage VB_TSC2631 with Unique N-Terminal Extension Used For Peptidoglycan Binding. Sci Rep V. 9 1261 2019.
Page generated: Mon Oct 28 21:04:30 2024
ISSN: ESSN 2045-2322 PubMed: 30718611 DOI: 10.1038/S41598-018-37417-6 |
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