5OK4
Crystal structure of native [Fe]-hydrogenase Hmd from Methanothermobacter marburgensis inactivated by O2.
Summary for 5OK4
Entry DOI | 10.2210/pdb5ok4/pdb |
Descriptor | 5,10-methenyltetrahydromethanopterin hydrogenase, FE (III) ION, 5'-O-[(S)-{[2-(carboxymethyl)-6-hydroxy-3,5-dimethylpyridin-4-yl]oxy}(hydroxy)phosphoryl]guanosine, ... (5 entities in total) |
Functional Keywords | [fe]-hydrogenase, fe-guanylylpyridinol cofactor, h2, hydrogenase, methanogenesis, methenyl-tetrahydromethanopterin, methylene-tetrahydromethanopterin, hydrogenation, o2, inactivation, oxidoreductase |
Biological source | Methanothermobacter marburgensis str. Marburg |
Total number of polymer chains | 1 |
Total formula weight | 38494.97 |
Authors | Wagner, T.,Huang, G.,Bill, E.,Ermler, U.,Ataka, K.,Shima, S. (deposition date: 2017-07-25, release date: 2018-05-16, Last modification date: 2024-01-17) |
Primary citation | Huang, G.,Wagner, T.,Ermler, U.,Bill, E.,Ataka, K.,Shima, S. Dioxygen Sensitivity of [Fe]-Hydrogenase in the Presence of Reducing Substrates. Angew. Chem. Int. Ed. Engl., 57:4917-4920, 2018 Cited by PubMed: 29462510DOI: 10.1002/anie.201712293 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.29 Å) |
Structure validation
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