6HUX
HmdII from Methanocaldococcus jannaschii reconstitued with Fe-guanylylpyridinol (FeGP) cofactor and co-crystallized with methenyl-tetrahydromethanopterin at 2.5 A resolution
Summary for 6HUX
Entry DOI | 10.2210/pdb6hux/pdb |
Descriptor | H(2)-forming methylenetetrahydromethanopterin dehydrogenase-related protein MJ1338, ACETATE ION, iron-guanylyl pyridinol cofactor, ... (10 entities in total) |
Functional Keywords | hydrogenase, h2-activation, lateral gene-transfer, cofactor biosynthesis, tetrahydromethanopterin, paralog, methanogen, metalloenzyme, oxidoreductase |
Biological source | Methanocaldococcus jannaschii DSM 2661 (Methanococcus jannaschii) |
Total number of polymer chains | 1 |
Total formula weight | 43610.64 |
Authors | Watanabe, T.,Wagner, T.,Huang, G.,Kahnt, J.,Ataka, K.,Ermler, U.,Shima, S. (deposition date: 2018-10-09, release date: 2019-01-09, Last modification date: 2024-01-24) |
Primary citation | Watanabe, T.,Wagner, T.,Huang, G.,Kahnt, J.,Ataka, K.,Ermler, U.,Shima, S. The Bacterial [Fe]-Hydrogenase Paralog HmdII Uses Tetrahydrofolate Derivatives as Substrates. Angew. Chem. Int. Ed. Engl., 58:3506-3510, 2019 Cited by PubMed: 30600878DOI: 10.1002/anie.201813465 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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