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5O4M

Fresh crystals of HcgC from Methanococcus maripaludis cocrystallized with SAH and pyridinol

Summary for 5O4M
Entry DOI10.2210/pdb5o4m/pdb
DescriptorHcgC, S-ADENOSYL-L-HOMOCYSTEINE, 6-carboxy methyl-4-hydroxy-2-pyridinol, ... (6 entities in total)
Functional Keywordsmethyltransferases, biosynthesis, protein structures, enzyme catalysis, mutagenesis, [fe]-hydrogenase, pyridinol, hmd, transferase
Biological sourceMethanococcus maripaludis S2
Total number of polymer chains4
Total formula weight126866.05
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 citationBai, 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: 28682478
DOI: 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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