1frv

CRYSTAL STRUCTURE OF THE OXIDIZED FORM OF NI-FE HYDROGENASE

spinqualitylabelsall models 1frv, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1frv is a 4 chain structure with sequence from Megalodesulfovibrio gigas. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.85Å Ligands: FEL, NI Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PHNS_MEGGA Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The X-ray structure of the heterodimeric Ni-Fe hydrogenase from Desulfovibrio gigas, the enzyme responsible for the metabolism of molecular hydrogen, has been solved at 2.85 A resolution. The active site, which appears to contain, besides nickel, a second metal ion, is buried in the 60K subunit. The 28K subunit, which coordinates one [3Fe-4S] and two [4Fe-4S] clusters, contains an amino-terminal domain with similarities to the redox protein flavodoxin. The structure suggests plausible electron and proton transfer pathways. Crystal structure of the nickel-iron hydrogenase from Desulfovibrio gigas.,Volbeda A, Charon MH, Piras C, Hatchikian EC, Frey M, Fontecilla-Camps JC Nature. 1995 Feb 16;373(6515):580-7. PMID:7854413 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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