Table 5. Structural comparison of mARH3 using the search algorithms from DALI (Holm & Sander, 1996 ▶) and SSM (Krissinel & Henrick, 2004 ▶).

Only results with a Z score higher than 2 are listed. The superposition of mARH3 with the corresponding protein was performed with the brute-force method implemented in the program LSQMAN (Novotny et al., 2004 ▶), from which the number of superimposed amino-acid residues, r.m.s. deviation and r.m.s. ΔB factor values were taken.

Protein name	Organism	PDB code	Annotated function	Space group	Resolution (Å)	No. of amino-acid residues	No. of superimposed Cα positions	Z score	R.m.s. deviation (Å)	R.m.s. ΔB factor (Å2)	Reference†
ADP-ribosylhydrolase 3	H. sapiens	2g4k	De-ADP-ribosylation	P212121	1.82	336	336	63.3‡, 15.7§	0.47	14.5	a
ADP-ribosylhydrolase 3	H. sapiens	2fp0	De-ADP-ribosylation	P21	2.05	335	335	15.9§	0.58	30.0	b
ADP-ribosylhydrolase 3	H. sapiens	2foz	De-ADP-ribosylation	P212121	1.60	336	336	15.9§	0.40	6.2	b
Ribosylglycohydrolase MJ1187	Methanococcus jannaschii	1t5j	Unknown	P43212	2.70	301	246	9.4§	1.36	34.1	c
ADP-ribosylglycohydrolase	T. thermophilus HB8	2cwc	De-ADP-ribosylation	P212121	1.65	303	240	8.5§	1.44	6.5	d
ADP-ribosylglycohydrolase	T. thermophilus HB8	2yzw	De-ADP-ribosylation	P212121	1.70	303	241	8.5§	1.30	6.8	e
ADP-ribosylglycohydrolase	T. thermophilus HB8	2yzv	De-ADP-ribosylation	P212121	1.60	303	241	8.4§	1.42	6.4	e
Methyl-coenzyme M reductase	Methanobacterium thermoautotrophicum	1mro	Methanogenesis	P21	1.16	548	69	4.2‡	2.14	4.4	f
Hat domain of murine CstF-77	Mus musculus	2ooe	Polyadenylation of mRNA precursors	H32	3.00	400	54	2.5‡	2.22	40.3	g

^†(a) Mueller-Dieckmann et al. (2007 ▶); (b) Mueller-Dieckmann et al. (2006 ▶); (c) deposited in the PDB 11 May 2004; (d) deposited in the PDB 18 June 2005; (e) deposited in the PDB 6 November 2007; (f) Ermler et al. (1997 ▶); (g) Bai et al. (2007 ▶).

^‡Results from DALI.

^§Results from SSM.