Literature summary for 1.1.1.146 extracted from

Favia, A.; Masetti, M.; Recanatini, M.; Cavalli, A.
Substrate binding process and mechanistic functioning of type 1 11beta-hydroxysteroid dehydrogenase from enhanced sampling methods (2011), PLoS ONE, 6, e25375.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
docking of cortisone into the catalytic site of wild type and mutant Y177A, PDB entry 2BEL. The catalytic site is stabilised in the enzyme dimer. Residues K44, N123, and T222 at the bottom of the cavity define a small functional back-door that allows water to enter or exit, making it easier for the substrate to leave or occupy the site. Residue Y177 is involved in stabilising interactions with the A ring of the substrate	Homo sapiens

Crystallization (Comment)

Organism

docking of cortisone into the catalytic site of wild type and mutant Y177A, PDB entry 2BEL. The catalytic site is stabilised in the enzyme dimer. Residues K44, N123, and T222 at the bottom of the cavity define a small functional back-door that allows water to enter or exit, making it easier for the substrate to leave or occupy the site. Residue Y177 is involved in stabilising interactions with the A ring of the substrate

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P28845	-	-

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Release 2023.1 (January 2023)