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Atomistry » Manganese » PDB 7z03-8awv » 7zz6 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Manganese » PDB 7z03-8awv » 7zz6 » |
Manganese in PDB 7zz6: Cryo-Em Structure of "Ct-Ct Dimer" of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-CoaEnzymatic activity of Cryo-Em Structure of "Ct-Ct Dimer" of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa
All present enzymatic activity of Cryo-Em Structure of "Ct-Ct Dimer" of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa:
6.4.1.1; Other elements in 7zz6:
The structure of Cryo-Em Structure of "Ct-Ct Dimer" of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa also contains other interesting chemical elements:
Manganese Binding Sites:
The binding sites of Manganese atom in the Cryo-Em Structure of "Ct-Ct Dimer" of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa
(pdb code 7zz6). This binding sites where shown within
5.0 Angstroms radius around Manganese atom.
In total 2 binding sites of Manganese where determined in the Cryo-Em Structure of "Ct-Ct Dimer" of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa, PDB code: 7zz6: Jump to Manganese binding site number: 1; 2; Manganese binding site 1 out of 2 in 7zz6Go back to Manganese Binding Sites List in 7zz6
Manganese binding site 1 out
of 2 in the Cryo-Em Structure of "Ct-Ct Dimer" of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa
Mono view Stereo pair view
Manganese binding site 2 out of 2 in 7zz6Go back to Manganese Binding Sites List in 7zz6
Manganese binding site 2 out
of 2 in the Cryo-Em Structure of "Ct-Ct Dimer" of Lactococcus Lactis Pyruvate Carboxylase with Acetyl-Coa
Mono view Stereo pair view
Reference:
J.P.Lopez-Alonso,
M.Lazaro,
D.Gil-Carton,
P.H.Choi,
A.Dodu,
L.Tong,
M.Valle.
Cryoem Structural Exploration of Catalytically Active Enzyme Pyruvate Carboxylase. Nat Commun V. 13 6185 2022.
Page generated: Sun Oct 6 11:15:17 2024
ISSN: ESSN 2041-1723 PubMed: 36261450 DOI: 10.1038/S41467-022-33987-2 |
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