3F46
The Crystal Structure of C176A Mutated [Fe]-Hydrogenase (Hmd) Holoenzyme from Methanocaldococcus jannaschii
Summary for 3F46
Entry DOI | 10.2210/pdb3f46/pdb |
Related | 2B0J 3DAF 3DAG 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, ... (6 entities in total) |
Functional Keywords | rossmann fold, helix bundle, complex with iron guanylyl pyridinol cofactor, c176a mutant, methanogenesis, one-carbon metabolism, oxidoreductase |
Biological source | Methanocaldococcus jannaschii (Methanococcus jannaschii) |
Total number of polymer chains | 1 |
Total formula weight | 39499.51 |
Authors | Hiromoto, T.,Vogt, S.,Warkentin, E.,Thauer, R.K.,Shima, S.,Ermler, U. (deposition date: 2008-10-31, release date: 2009-02-10, Last modification date: 2023-11-01) |
Primary citation | Hiromoto, T.,Ataka, K.,Pilak, O.,Vogt, S.,Stagni, M.S.,Meyer-Klaucke, W.,Warkentin, E.,Thauer, R.K.,Shima, S.,Ermler, U. The crystal structure of C176A mutated [Fe]-hydrogenase suggests an acyl-iron ligation in the active site iron complex. Febs Lett., 583:585-590, 2009 Cited by PubMed: 19162018DOI: 10.1016/j.febslet.2009.01.017 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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