3H65
The Crystal Structure of C176A Mutated [Fe]-Hydrogenase (Hmd) Holoenzyme in Complex with Methylenetetrahydromethanopterin
Summary for 3H65
Entry DOI | 10.2210/pdb3h65/pdb |
Related | 2B0J 3F46 3F47 |
Descriptor | 5,10-methenyltetrahydromethanopterin hydrogenase, 5'-O-[(S)-hydroxy{[2-hydroxy-3,5-dimethyl-6-(2-oxoethyl)pyridin-4-yl]oxy}phosphoryl]guanosine, FE (II) ION, ... (7 entities in total) |
Functional Keywords | rossmann fold, helix bundle, complex with iron guanylyl pyridinol cofactor, c176a mutant, complex with methylenetetrahydromethanopterin, methanogenesis, one-carbon metabolism, oxidoreductase |
Biological source | Methanocaldococcus jannaschii (Methanococcus jannaschii) |
Total number of polymer chains | 1 |
Total formula weight | 40288.21 |
Authors | Hiromoto, T.,Warkentin, E.,Shima, S.,Ermler, U. (deposition date: 2009-04-23, release date: 2009-09-01, Last modification date: 2023-11-01) |
Primary citation | Hiromoto, T.,Warkentin, E.,Moll, J.,Ermler, U.,Shima, S. The crystal structure of an [Fe]-hydrogenase-substrate complex reveals the framework for H2 activation. Angew.Chem.Int.Ed.Engl., 48:6457-6460, 2009 Cited by PubMed: 19623593DOI: 10.1002/anie.200902695 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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