1EUG

CRYSTAL STRUCTURE OF ESCHERICHIA COLI URACIL DNA GLYCOSYLASE AND ITS COMPLEXES WITH URACIL AND GLYCEROL: STRUCTURE AND GLYCOSYLASE MECHANISM REVISITED

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004844	molecular_function	uracil DNA N-glycosylase activity
A	0005515	molecular_function	protein binding
A	0005737	cellular_component	cytoplasm
A	0006281	biological_process	DNA repair
A	0006284	biological_process	base-excision repair
A	0016787	molecular_function	hydrolase activity
A	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
A	0097510	biological_process	base-excision repair, AP site formation via deaminated base removal

Functional Information from PROSITE/UniProt

site_id	PS00130
Number of Residues	10
Details	U_DNA_GLYCOSYLASE Uracil-DNA glycosylase signature. KVVIlGQDPY

Chain	Residue	Details
A	LYS57-TYR66

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor

Chain	Residue	Details
A	ASP64

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Catalytic Information from CSA

site_id	MCSA1
Number of Residues	4
Details	M-CSA 71

Chain	Residue	Details
A	ASP64	activator, electrostatic stabiliser, increase acidity, proton acceptor, proton donor
A	TYR66	activator, steric role
A	PHE77	activator, steric role
A	HIS187	covalently attached, electrostatic stabiliser, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor

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