Literature summary for 1.13.11.19 extracted from

Wang, Y.; Shin, I.; Li, J.; Liu, A.
Crystal structure of human cysteamine dioxygenase provides a structural rationale for its function as an oxygen sensor (2021), J. Biol. Chem., 297, 34508780 .

Search for more literature for 1.13.11.19

Application

Application	Comment	Organism
medicine	ADO functions as an oxygen sensor by modifying N-degron substrates to transduce responses to hypoxia	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of human ADO at a resolution of 1.78 A with a nickel-bound metal center. Crystallization is achieved through both metal substitution and C18S/C239S double mutations. The metal center resides in a tunnel close to an entry site flanked by loops. ADO appears to use extensive flexibility to handle substrates of different sizes, and also employs proline and proline pairs to maintain the core protein structure and to retain the residues critical for catalysis in place	Homo sapiens

Crystallization (Comment)

Organism

structure of human ADO at a resolution of 1.78 A with a nickel-bound metal center. Crystallization is achieved through both metal substitution and C18S/C239S double mutations. The metal center resides in a tunnel close to an entry site flanked by loops. ADO appears to use extensive flexibility to handle substrates of different sizes, and also employs proline and proline pairs to maintain the core protein structure and to retain the residues critical for catalysis in place

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
C18S/C239S	mutations of surface residues introduced for crystallization	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q96SZ5	-	-

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Release 2023.1 (January 2023)