1CC1

CRYSTAL STRUCTURE OF A REDUCED, ACTIVE FORM OF THE NI-FE-SE HYDROGENASE FROM DESULFOMICROBIUM BACULATUM

Summary for 1CC1

Entry DOI	10.2210/pdb1cc1/pdb
Descriptor	HYDROGENASE (SMALL SUBUNIT), HYDROGENASE (LARGE SUBUNIT), IRON/SULFUR CLUSTER, ... (8 entities in total)
Functional Keywords	ni-fe-se hydrogenase, oxidoreductase
Biological source	Desulfomicrobium baculatum More
Total number of polymer chains	2
Total formula weight	87445.39
Authors	Garcin, E.,Vernede, X.,Hatchikian, E.C.,Volbeda, A.,Frey, M.,Fontecilla-Camps, J.C. (deposition date: 1999-03-03, release date: 1999-06-01, Last modification date: 2023-08-09)
Primary citation	Garcin, E.,Vernede, X.,Hatchikian, E.C.,Volbeda, A.,Frey, M.,Fontecilla-Camps, J.C. The crystal structure of a reduced [NiFeSe] hydrogenase provides an image of the activated catalytic center Structure Fold.Des., 7:557-566, 1999 Cited by PubMed Abstract: [NiFeSe] hydrogenases are metalloenzymes that catalyze the reaction H2<-->2H+ + 2e-. They are generally heterodimeric, contain three iron-sulfur clusters in their small subunit and a nickel-iron-containing active site in their large subunit that includes a selenocysteine (SeCys) ligand. PubMed: 10378275 DOI: 10.1016/S0969-2126(99)80072-0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.15 Å)

Structure validation