5O4M
Fresh crystals of HcgC from Methanococcus maripaludis cocrystallized with SAH and pyridinol
Summary for 5O4M
Entry DOI | 10.2210/pdb5o4m/pdb |
Descriptor | HcgC, S-ADENOSYL-L-HOMOCYSTEINE, 6-carboxy methyl-4-hydroxy-2-pyridinol, ... (6 entities in total) |
Functional Keywords | methyltransferases, biosynthesis, protein structures, enzyme catalysis, mutagenesis, [fe]-hydrogenase, pyridinol, hmd, transferase |
Biological source | Methanococcus maripaludis S2 |
Total number of polymer chains | 4 |
Total formula weight | 126866.05 |
Authors | Wagner, T.,Bai, L.,Xu, T.,Hu, X.,Ermler, U.,Shima, S. (deposition date: 2017-05-29, release date: 2017-07-19, Last modification date: 2024-01-17) |
Primary citation | Bai, L.,Wagner, T.,Xu, T.,Hu, X.,Ermler, U.,Shima, S. A Water-Bridged H-Bonding Network Contributes to the Catalysis of the SAM-Dependent C-Methyltransferase HcgC. Angew. Chem. Int. Ed. Engl., 56:10806-10809, 2017 Cited by PubMed: 28682478DOI: 10.1002/anie.201705605 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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