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EC Number	Crystallization (Commentary)
1.14.13.172	structure of the oxygenase component NagGH. The large subunit NagG and small subunit NagH share the same fold as that for their counterparts of Rieske dioxygenases and assemble the same alpha3beta3 hexamer. A potential substrate-binding pocket is observed in the vicinity of the nonheme iron site. Its positively charged residue Arg323 is surrounded by hydrophobic residues. The shift of nonheme iron atom caused by residue Leu228 disrupts the usual substrate pocket observed in other Rieske oxygenases. Residue Asn218 is involved in substrate binding and oxidation, but residues Gln316 and Ser367 play a more important role in substrate oxidation than Asn218

EC Number

Crystallization (Commentary)

1.14.13.172

structure of the oxygenase component NagGH. The large subunit NagG and small subunit NagH share the same fold as that for their counterparts of Rieske dioxygenases and assemble the same alpha3beta3 hexamer. A potential substrate-binding pocket is observed in the vicinity of the nonheme iron site. Its positively charged residue Arg323 is surrounded by hydrophobic residues. The shift of nonheme iron atom caused by residue Leu228 disrupts the usual substrate pocket observed in other Rieske oxygenases. Residue Asn218 is involved in substrate binding and oxidation, but residues Gln316 and Ser367 play a more important role in substrate oxidation than Asn218

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Release 2023.1 (January 2023)