3NT7

Crystal Structure of Vaccinia Virus Uracil DNA Glycosylase R187V Mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0004844	molecular_function	uracil DNA N-glycosylase activity
A	0006281	biological_process	DNA repair
A	0006974	biological_process	DNA damage response
A	0016787	molecular_function	hydrolase activity
A	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds
C	0003677	molecular_function	DNA binding
C	0004844	molecular_function	uracil DNA N-glycosylase activity
C	0006281	biological_process	DNA repair
C	0006974	biological_process	DNA damage response
C	0016787	molecular_function	hydrolase activity
C	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 C 219

Chain	Residue
C	GLY159
C	LYS160
C	THR161
C	TYR180
C	HIS181

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 C 220

Chain	Residue
A	ARG98
A	HOH238
C	ARG98

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site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE GOL C 221

Chain	Residue
C	ASN199

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site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 219

Chain	Residue
A	GLY159
A	LYS160
A	TYR180
A	HIS181

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	ARG61-TYR70

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU10072","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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