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: 29462510 DOI: 10.1002/anie.201712293 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.29 Å)

Structure validation