3TKB

crystal structure of human uracil-DNA glycosylase D183G/K302R mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004844	molecular_function	uracil DNA N-glycosylase activity
A	0006281	biological_process	DNA repair
A	0006284	biological_process	base-excision repair
A	0016799	molecular_function	hydrolase activity, hydrolyzing N-glycosyl compounds

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IMD A 4496

Chain	Residue
A	GLY280
A	ARG282
A	LYS286

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE IMD A 305

Chain	Residue
A	HOH29
A	LYS175
A	PHE279

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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	LYS138-TYR147

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_03166","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9724657","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SSP","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8900285","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9724657","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SSP","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"4SKN","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"8900285","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4SKN","evidenceCode":"ECO:0000312"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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