3QI5

Crystal structure of human alkyladenine DNA glycosylase in complex with 3,N4-ethenocystosine containing duplex DNA

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Pharos: Disease Associations

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3qi5a1	All beta proteins	FMT C-terminal domain-like	FMT C-terminal domain-like	3-methyladenine DNA glycosylase (AAG, ANPG, MPG)	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
A	d3qi5a2	Artifacts	Tags	Tags	Tags	N-terminal Tags	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d3qi5b1	All beta proteins	FMT C-terminal domain-like	FMT C-terminal domain-like	3-methyladenine DNA glycosylase (AAG, ANPG, MPG)	automated matches	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d3qi5b2	Artifacts	Tags	Tags	Tags	N-terminal Tags	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	FMT C-terminal domain-like	8002457	3000015	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	FMT C-terminal domain-like	8002457	3000015	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Pur_DNA_glyco	e3qi5A1	A: beta barrels	X: FMT C-terminal domain-like	H: FMT C-terminal domain-related (From Topology)	T: FMT C-terminal domain-related	F: Pur_DNA_glyco	ECOD (1.6)
B	Pur_DNA_glyco	e3qi5B1	A: beta barrels	X: FMT C-terminal domain-like	H: FMT C-terminal domain-related (From Topology)	T: FMT C-terminal domain-related	F: Pur_DNA_glyco	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.10.300.10	Alpha Beta	Roll	3-methyladenine DNA Glycosylase	Chain A	CATH (4.3.0)
B	3.10.300.10	Alpha Beta	Roll	3-methyladenine DNA Glycosylase	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF02245	Methylpurine-DNA glycosylase (MPG) (Pur_DNA_glyco)	Methylpurine-DNA glycosylase (MPG)	Methylpurine-DNA glycosylase is a base excision-repair protein. It is responsible for the hydrolysis of the deoxyribose N-glycosidic bond, excising 3-methyladenine and 3-methylguanine from damaged DNA.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	DNA-3-methyladenine glycosylase	alkylbase DNA N-glycosylase activity hydrolase activity, acting on glycosyl bonds catalytic activity, acting on DNA catalytic activity, acting on a nucleic acid hydrolase activity DNA N-glycosylase activity hydrolase activity, hydrolyzing N-glycosyl compounds catalytic activity DNA-3-methylguanine glycosylase activity DNA-3-methylbase glycosylase activity DNA-3-methyladenine glycosylase activity DNA-7-methyladenine glycosylase activity DNA binding binding alkylbase DNA N-glycosylase activity hydrolase activity, acting on glycosyl bonds catalytic activity, acting on DNA catalytic activity, acting on a nucleic acid hydrolase activity DNA N-glycosylase activity hydrolase activity, hydrolyzing N-glycosyl compounds catalytic activity DNA-3-methylguanine glycosylase activity DNA-3-methylbase glycosylase activity DNA-3-methyladenine glycosylase activity DNA-7-methyladenine glycosylase activity DNA binding binding organic cyclic compound binding damaged DNA binding nucleic acid binding DNA-7-methylguanine glycosylase activity	cellular response to stimulus response to stimulus primary metabolic process DNA metabolic process nucleic acid metabolic process nucleobase-containing compound metabolic process base-excision repair DNA modification cellular response to stress DNA damage response depurination response to stress macromolecule modification metabolic process cellular response to stimulus response to stimulus primary metabolic process DNA metabolic process nucleic acid metabolic process nucleobase-containing compound metabolic process base-excision repair DNA modification cellular response to stress DNA damage response depurination response to stress macromolecule modification metabolic process cellular process macromolecule metabolic process base-excision repair, AP site formation DNA repair DNA alkylation repair	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle cytosol membrane-enclosed lumen intracellular membraneless organelle nucleoid mitochondrial matrix intracellular organelle lumen membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure mitochondrion organelle cytoplasm intracellular membrane-bounded organelle cytosol membrane-enclosed lumen intracellular membraneless organelle nucleoid mitochondrial matrix intracellular organelle lumen organelle lumen membraneless organelle mitochondrial nucleoid nucleus nucleoplasm nuclear lumen
C, E	DNA (5'-D(GPAPCPAPTPGP(EDC)PTPTPGPCPCP*T)-3')	-	-	-
D, F	DNA (5'-D(GPGPCPAPAPGPCPAPTPGPTPCP*A)-3')	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036995	Methylpurine-DNA glycosylase superfamily	Homologous Superfamily
A, B	IPR011034	Formyl transferase-like, C-terminal domain superfamily	Homologous Superfamily
A, B	IPR003180	Methylpurine-DNA glycosylase	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B	Pharos: P29372	glioblastoma osteosarcoma spina bifida

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.