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Atomistry » Zinc » PDB 9bzp-9ci7 » 9ch3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Zinc » PDB 9bzp-9ci7 » 9ch3 » |
Zinc in PDB 9ch3: Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona-L63D) Heteromeric Complex (Bound to Sah)Protein crystallography data
The structure of Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona-L63D) Heteromeric Complex (Bound to Sah), PDB code: 9ch3
was solved by
K.K.Crone,
J.W.Labonte,
M.Elias,
M.F.Freeman,
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 Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona-L63D) Heteromeric Complex (Bound to Sah)
(pdb code 9ch3). 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 the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona-L63D) Heteromeric Complex (Bound to Sah), PDB code: 9ch3: Jump to Zinc binding site number: 1; 2; Zinc binding site 1 out of 2 in 9ch3Go back to![]() ![]()
Zinc binding site 1 out
of 2 in the Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona-L63D) Heteromeric Complex (Bound to Sah)
![]() Mono view ![]() Stereo pair view
Zinc binding site 2 out of 2 in 9ch3Go back to![]() ![]()
Zinc binding site 2 out
of 2 in the Structure of the Alpha-N-Methyltransferase (Sonm) and Ripp Precursor (Sona-L63D) Heteromeric Complex (Bound to Sah)
![]() Mono view ![]() Stereo pair view
Reference:
K.K.Crone,
J.W.Labonte,
M.H.Elias,
M.F.Freeman.
Alpha-N-Methyltransferase Regiospecificity Is Mediated By Proximal, Redundant Enzyme-Substrate Interactions. Protein Sci. V. 34 70021 2025.
Page generated: Fri Aug 22 16:58:53 2025
ISSN: ESSN 1469-896X PubMed: 39840790 DOI: 10.1002/PRO.70021 |
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