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Atomistry » Molybdenum » PDB 8cff-9d2c » 8dbx | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Atomistry » Molybdenum » PDB 8cff-9d2c » 8dbx » |
Molybdenum in PDB 8dbx: Cryoem Structure of Partially Oxidized Mofe-Protein on Ultrathin CarbonEnzymatic activity of Cryoem Structure of Partially Oxidized Mofe-Protein on Ultrathin Carbon
All present enzymatic activity of Cryoem Structure of Partially Oxidized Mofe-Protein on Ultrathin Carbon:
1.18.6.1; Other elements in 8dbx:
The structure of Cryoem Structure of Partially Oxidized Mofe-Protein on Ultrathin Carbon also contains other interesting chemical elements:
Molybdenum Binding Sites:
The binding sites of Molybdenum atom in the Cryoem Structure of Partially Oxidized Mofe-Protein on Ultrathin Carbon
(pdb code 8dbx). This binding sites where shown within
5.0 Angstroms radius around Molybdenum atom.
In total 2 binding sites of Molybdenum where determined in the Cryoem Structure of Partially Oxidized Mofe-Protein on Ultrathin Carbon, PDB code: 8dbx: Jump to Molybdenum binding site number: 1; 2; Molybdenum binding site 1 out of 2 in 8dbxGo back to Molybdenum Binding Sites List in 8dbx
Molybdenum binding site 1 out
of 2 in the Cryoem Structure of Partially Oxidized Mofe-Protein on Ultrathin Carbon
Mono view Stereo pair view
Molybdenum binding site 2 out of 2 in 8dbxGo back to Molybdenum Binding Sites List in 8dbx
Molybdenum binding site 2 out
of 2 in the Cryoem Structure of Partially Oxidized Mofe-Protein on Ultrathin Carbon
Mono view Stereo pair view
Reference:
R.A.Warmack,
A.O.Maggiolo,
A.Orta,
B.B.Wenke,
J.B.Howard,
D.C.Rees.
Structural Consequences of Turnover-Induced Homocitrate Loss in Nitrogenase. Nat Commun V. 14 1091 2023.
Page generated: Sun Oct 6 17:40:00 2024
ISSN: ESSN 2041-1723 PubMed: 36841829 DOI: 10.1038/S41467-023-36636-4 |
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