9N2P
Structure of MoaC-covalent intermediate complex obtained in the presence of Mg.
This is a non-PDB format compatible entry.
Summary for 9N2P
| Entry DOI | 10.2210/pdb9n2p/pdb |
| Descriptor | Cyclic pyranopterin monophosphate synthase, [(2~{R},3~{R})-4-(2-azanyl-4-oxidanylidene-5,8-dihydro-3~{H}-pteridin-6-yl)-2,3-bis(oxidanyl)butoxy]-[[oxidanyl(phosphonooxy)phosphoryl]methyl]phosphinic acid, MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | moac, moaa, enzyme, intermediate, biosynthetic protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 17988.58 |
| Authors | |
| Primary citation | Li, D.,Schumacher, M.A.,Yokoyama, K. Covalent carbon-tethering mechanism guides a complex rearrangement in molybdenum cofactor biosynthesis To Be Published, |
| Experimental method | X-RAY DIFFRACTION (2.26 Å) |
Structure validation
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