Literature summary for 1.14.11.54 extracted from

Sundheim, O.; Vagbo, C.; Bjoras, M.; Sousa, M.; Talstad, V.; Aas, P.; Drablos, F.; Krokan, H.; Tainer, J.; Slupphaug, G.
Human ABH3 structure and key residues for oxidative demethylation to reverse DNA/RNA damage (2006), EMBO J., 25, 3389-3397.

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure of the ABH3 catalytic core in complex with iron and 2-oxoglutarate at 1.5 A resolution. The ABH3 structure reveals the beta-strand jelly-roll fold that coordinates a catalytically active iron centre by a conserved His1-X-Asp/Glu-Xn-His2 motif. The structure shows a positively charged DNA/RNA binding groove and a flexible hairpin involved in nucleotide flipping and ss/ds-DNA discrimination, and reveals self-hydroxylation of an active site leucine	Homo sapiens

Crystallization (Comment)

Organism

structure of the ABH3 catalytic core in complex with iron and 2-oxoglutarate at 1.5 A resolution. The ABH3 structure reveals the beta-strand jelly-roll fold that coordinates a catalytically active iron centre by a conserved His1-X-Asp/Glu-Xn-His2 motif. The structure shows a positively charged DNA/RNA binding groove and a flexible hairpin involved in nucleotide flipping and ss/ds-DNA discrimination, and reveals self-hydroxylation of an active site leucine

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q96Q83	-	-

Synonyms

Synonyms	Comment	Organism
ABH3	-	Homo sapiens

General Information

General Information	Comment	Organism
physiological function	1-methyladenine and 3-methylcytosine lesions in DNA/RNA contribute to the cytotoxicity of methylating agents. These lesions are directly reversed by ABH3 in humans	Homo sapiens

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Release 2023.1 (January 2023)