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Atomistry » Zinc » PDB 4w8y-4wnu » 4w8y | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 4w8y-4wnu » 4w8y » |
Zinc in PDB 4w8y: Structure of Full Length CMR2 From Pyrococcus Furiosus (Manganese Bound Form)Protein crystallography data
The structure of Structure of Full Length CMR2 From Pyrococcus Furiosus (Manganese Bound Form), PDB code: 4w8y
was solved by
C.Benda,
J.Ebert,
M.Baumgaertner,
E.Conti,
with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:
Other elements in 4w8y:
The structure of Structure of Full Length CMR2 From Pyrococcus Furiosus (Manganese Bound Form) also contains other interesting chemical elements:
Zinc Binding Sites:
The binding sites of Zinc atom in the Structure of Full Length CMR2 From Pyrococcus Furiosus (Manganese Bound Form)
(pdb code 4w8y). This binding sites where shown within
5.0 Angstroms radius around Zinc atom.
In total 2 binding sites of Zinc where determined in the Structure of Full Length CMR2 From Pyrococcus Furiosus (Manganese Bound Form), PDB code: 4w8y: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 4w8yGo back to![]() ![]()
Zinc binding site 1 out
of 2 in the Structure of Full Length CMR2 From Pyrococcus Furiosus (Manganese Bound Form)
![]() Mono view ![]() Stereo pair view
Zinc binding site 2 out of 2 in 4w8yGo back to![]() ![]()
Zinc binding site 2 out
of 2 in the Structure of Full Length CMR2 From Pyrococcus Furiosus (Manganese Bound Form)
![]() Mono view ![]() Stereo pair view
Reference:
C.Benda,
J.Ebert,
R.A.Scheltema,
H.B.Schiller,
M.Baumgartner,
F.Bonneau,
M.Mann,
E.Conti.
Structural Model of A Crispr Rna-Silencing Complex Reveals the Rna-Target Cleavage Activity in CMR4. Mol.Cell V. 56 43 2014.
Page generated: Sun Oct 27 09:43:50 2024
ISSN: ISSN 1097-2765 PubMed: 25280103 DOI: 10.1016/J.MOLCEL.2014.09.002 |
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