Literature summary for 2.3.2.27 extracted from

Spratt, D.E.;, Mercier, P.; Shaw, G.S.
Structure of the HHARI catalytic domain shows glimpses of a HECT E3 ligase (2013), PLoS One, 15, e74047.

Crystallization (Commentary)

Crystallization (Comment)	Organism
solution structure of the isoform HHARI RING2 domain, the key portion of this E3 ligase required for the RING/HECT hybrid mechanism. The domain possesses two Zn2+-binding sites and a single exposed cysteine used for ubiquitin catalysis. A structural comparison of the RING2 domain with the HECT E3 ligase NEDD4 reveals a near mirror image of the cysteine and histidine residues in the catalytic site. A tandem pair of aromatic residues exists near the C-terminus of the HHARI RING2 domain that is conserved in other RING-in-Between-RING E3 ligases	Homo sapiens

Crystallization (Comment)

Organism

solution structure of the isoform HHARI RING2 domain, the key portion of this E3 ligase required for the RING/HECT hybrid mechanism. The domain possesses two Zn2+-binding sites and a single exposed cysteine used for ubiquitin catalysis. A structural comparison of the RING2 domain with the HECT E3 ligase NEDD4 reveals a near mirror image of the cysteine and histidine residues in the catalytic site. A tandem pair of aromatic residues exists near the C-terminus of the HHARI RING2 domain that is conserved in other RING-in-Between-RING E3 ligases

Homo sapiens

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zinc	two Zn2+-binding sites are present involving four cysteine residues found in the loops between beta1-beta2 and beta3-beta4 at site I, residues C344, C347, C362, C367, and three cysteines and a histidine in the extended loop after beta4 at site II, residues C372, C375, H382, C389	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9Y4X5	isoform HHARI	-

Synonyms

Synonyms	Comment	Organism
ARIH1	-	Homo sapiens
HHARI	-	Homo sapiens
Human Homologue of Drosophila Ariadne	-	Homo sapiens

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Release 2023.1 (January 2023)