2.3.2.27	As3+	As3+ can bind to the PHD/RING finger domain of FANCL in vitro and in cells. This binding leads to compromised ubiquitination of FANCD2 in cells and diminishes recruitment of FANCD2 to chromatin and DNA damage sites induced by 4,5',8-trimethylpsoralen plus UVA irradiation	4502	
2.3.2.27	DTPA	treatment leads to inactivation	135273	
2.3.2.27	EDTA	treatment leads to inactivation	21	
2.3.2.27	MLN4924	Nedd8 activating enzyme (NAE1) inhibitor, interferes with the activation of all cullin E3-ligases	247441	
2.3.2.27	additional information	E3 ubiquitin ligase activity of isoform RBCK1 is inhibited by interaction with splice variant RBCK2	2	
2.3.2.27	additional information	binding of the RAPTA compounds, i.e. Ru(h6-arene)(1,3,5-triaza-7-phosphaadamantane)Cl2, to the BRCA1 protein results in a release of Zn2+ ions in a dose- and time-dependent manner, as well as thermal alteration of ruthenated-BRCA1 proteins. The preferential binding sites of the RAPTA complexes on the BRCA1 zinc finger RING domain are at a short peptide stretch, Cys24-Lys25-Phe26-Cys27-Met28-Leu29 and Lys35 (residues 44-49 and 55 on full length BRCA1). Binding results in inactivation of the RING heterodimer BRCA1/BARD1-mediated E3 ubiquitin ligase function	2	
2.3.2.27	RAPTA-C	-	75375	
2.3.2.27	RAPTA-EA1	the IC50 value for inactivation of E3 ubiquitin ligase activity by RAPTA-EA1 is markedly lower than the corresponding values for RAPTA-C, RAPTA-T and cisplatin	246912	
2.3.2.27	RAPTA-T	-	75373