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Zinc in PDB 4csa: Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to A Dna 4-MerProtein crystallography data
The structure of Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to A Dna 4-Mer, PDB code: 4csa
was solved by
C.Leyrat,
M.Renner,
K.Harlos,
J.M.Grimes,
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 Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to A Dna 4-Mer
(pdb code 4csa). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 4 binding sites of Zinc where determined in the Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to A Dna 4-Mer, PDB code: 4csa: Jump to Zinc binding site number: 1; 2; 3; 4; Zinc binding site 1 out of 4 in 4csaGo back to Zinc Binding Sites List in 4csa
Zinc binding site 1 out
of 4 in the Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to A Dna 4-Mer
Mono view Stereo pair view
Zinc binding site 2 out of 4 in 4csaGo back to Zinc Binding Sites List in 4csa
Zinc binding site 2 out
of 4 in the Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to A Dna 4-Mer
Mono view Stereo pair view
Zinc binding site 3 out of 4 in 4csaGo back to Zinc Binding Sites List in 4csa
Zinc binding site 3 out
of 4 in the Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to A Dna 4-Mer
Mono view Stereo pair view
Zinc binding site 4 out of 4 in 4csaGo back to Zinc Binding Sites List in 4csa
Zinc binding site 4 out
of 4 in the Crystal Structure of the Asymmetric Human Metapneumovirus M2-1 Tetramer Bound to A Dna 4-Mer
Mono view Stereo pair view
Reference:
C.Leyrat,
M.Renner,
K.Harlos,
J.T.Huiskonen,
J.M.Grimes.
Drastic Changes in Conformational Dynamics of the Antiterminator M2-1 Regulate Transcription Efficiency in Pneumovirinae. Elife V. 3 02674 2014.
Page generated: Wed Dec 16 05:09:19 2020
ISSN: ISSN 2050-084X PubMed: 24842877 DOI: 10.7554/ELIFE.02674 |
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