1LQM

ESCHERICHIA COLI URACIL-DNA GLYCOSYLASE COMPLEX WITH URACIL-DNA GLYCOSYLASE INHIBITOR PROTEIN

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1lqma_	Alpha and beta proteins (a/b)	Uracil-DNA glycosylase-like	Uracil-DNA glycosylase-like	Uracil-DNA glycosylase	Uracil-DNA glycosylase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1lqmc_	Alpha and beta proteins (a/b)	Uracil-DNA glycosylase-like	Uracil-DNA glycosylase-like	Uracil-DNA glycosylase	Uracil-DNA glycosylase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
E	d1lqme_	Alpha and beta proteins (a/b)	Uracil-DNA glycosylase-like	Uracil-DNA glycosylase-like	Uracil-DNA glycosylase	Uracil-DNA glycosylase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
G	d1lqmg_	Alpha and beta proteins (a/b)	Uracil-DNA glycosylase-like	Uracil-DNA glycosylase-like	Uracil-DNA glycosylase	Uracil-DNA glycosylase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1lqmb_	Alpha and beta proteins (a+b)	Cystatin-like	Uracil-DNA glycosylase inhibitor protein	Uracil-DNA glycosylase inhibitor protein	Uracil-DNA glycosylase inhibitor protein	(Bacillus phage PBS2 ) [TaxId: 10684 ],	SCOPe (2.08)
D	d1lqmd_	Alpha and beta proteins (a+b)	Cystatin-like	Uracil-DNA glycosylase inhibitor protein	Uracil-DNA glycosylase inhibitor protein	Uracil-DNA glycosylase inhibitor protein	(Bacillus phage PBS2 ) [TaxId: 10684 ],	SCOPe (2.08)
F	d1lqmf_	Alpha and beta proteins (a+b)	Cystatin-like	Uracil-DNA glycosylase inhibitor protein	Uracil-DNA glycosylase inhibitor protein	Uracil-DNA glycosylase inhibitor protein	(Bacillus phage PBS2 ) [TaxId: 10684 ],	SCOPe (2.08)
H	d1lqmh_	Alpha and beta proteins (a+b)	Cystatin-like	Uracil-DNA glycosylase inhibitor protein	Uracil-DNA glycosylase inhibitor protein	Uracil-DNA glycosylase inhibitor protein	(Bacillus phage PBS2 ) [TaxId: 10684 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Uracil-DNA glycosylase-like	8044008	3001106	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Uracil-DNA glycosylase-like	8044008	3001106	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Uracil-DNA glycosylase-like	8044008	3001106	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Uracil-DNA glycosylase-like	8044008	3001106	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Uracil-DNA glycosylase inhibitor protein	8034693	3000500	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Uracil-DNA glycosylase inhibitor protein	8034693	3000500	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Uracil-DNA glycosylase inhibitor protein	8034693	3000500	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Uracil-DNA glycosylase inhibitor protein	8034693	3000500	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	UDG	e1lqmA1	A: a/b three-layered sandwiches	X: Uracil-DNA glycosylase-like (From Topology)	H: Uracil-DNA glycosylase-like (From Topology)	T: Uracil-DNA glycosylase-like	F: UDG	ECOD (1.6)
C	UDG	e1lqmC1	A: a/b three-layered sandwiches	X: Uracil-DNA glycosylase-like (From Topology)	H: Uracil-DNA glycosylase-like (From Topology)	T: Uracil-DNA glycosylase-like	F: UDG	ECOD (1.6)
E	UDG	e1lqmE1	A: a/b three-layered sandwiches	X: Uracil-DNA glycosylase-like (From Topology)	H: Uracil-DNA glycosylase-like (From Topology)	T: Uracil-DNA glycosylase-like	F: UDG	ECOD (1.6)
G	UDG	e1lqmG1	A: a/b three-layered sandwiches	X: Uracil-DNA glycosylase-like (From Topology)	H: Uracil-DNA glycosylase-like (From Topology)	T: Uracil-DNA glycosylase-like	F: UDG	ECOD (1.6)
B	EUF08292	e1lqmB1	A: a+b two layers	X: Cystatin-like	H: Uracil-DNA glycosylase inhibitor protein (From Topology)	T: Uracil-DNA glycosylase inhibitor protein	F: EUF08292	ECOD (1.6)
D	EUF08292	e1lqmD1	A: a+b two layers	X: Cystatin-like	H: Uracil-DNA glycosylase inhibitor protein (From Topology)	T: Uracil-DNA glycosylase inhibitor protein	F: EUF08292	ECOD (1.6)
F	EUF08292	e1lqmF1	A: a+b two layers	X: Cystatin-like	H: Uracil-DNA glycosylase inhibitor protein (From Topology)	T: Uracil-DNA glycosylase inhibitor protein	F: EUF08292	ECOD (1.6)
H	EUF08292	e1lqmH1	A: a+b two layers	X: Cystatin-like	H: Uracil-DNA glycosylase inhibitor protein (From Topology)	T: Uracil-DNA glycosylase inhibitor protein	F: EUF08292	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.470.10	Alpha Beta	3-Layer(aba) Sandwich	Uracil-DNA Glycosylase, subunit E	Uracil-DNA glycosylase-like domain	CATH (4.3.0)
C	3.40.470.10	Alpha Beta	3-Layer(aba) Sandwich	Uracil-DNA Glycosylase, subunit E	Uracil-DNA glycosylase-like domain	CATH (4.3.0)
E	3.40.470.10	Alpha Beta	3-Layer(aba) Sandwich	Uracil-DNA Glycosylase, subunit E	Uracil-DNA glycosylase-like domain	CATH (4.3.0)
G	3.40.470.10	Alpha Beta	3-Layer(aba) Sandwich	Uracil-DNA Glycosylase, subunit E	Uracil-DNA glycosylase-like domain	CATH (4.3.0)
B	3.10.450.20	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (4.3.0)
D	3.10.450.20	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (4.3.0)
F	3.10.450.20	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (4.3.0)
H	3.10.450.20	Alpha Beta	Roll	Nuclear Transport Factor 2	Chain: A,	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, C, E, G	PF03167	Uracil DNA glycosylase superfamily (UDG)	Uracil DNA glycosylase superfamily	-	Domain
B, D, F, H	PF18880	Uracil-DNA glycosylase inhibitor (UDI)	Uracil-DNA glycosylase inhibitor	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, C, E, G	URACIL-DNA GLYCOSYLASE	uracil DNA N-glycosylase activity hydrolase activity, acting on glycosyl bonds deaminated base DNA N-glycosylase activity 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	cellular response to stimulus response to stimulus base-excision repair, AP site formation via deaminated base removal primary metabolic process DNA metabolic process nucleic acid metabolic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process base-excision repair organic substance metabolic process cellular response to stress DNA damage response response to stress metabolic process cellular response to stimulus response to stimulus base-excision repair, AP site formation via deaminated base removal primary metabolic process DNA metabolic process nucleic acid metabolic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process base-excision repair organic substance metabolic process cellular response to stress DNA damage response response to stress metabolic process cellular process macromolecule metabolic process base-excision repair, AP site formation DNA repair	intracellular anatomical structure cytoplasm cellular anatomical entity
B, D, F, H	URACIL-DNA GLYCOSYLASE INHIBITOR	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, C, E, G	IPR002043	Uracil-DNA glycosylase family 1	Family
A, C, E, G	IPR018085	Uracil-DNA glycosylase, active site	Active Site
A, C, E, G	IPR036895	Uracil-DNA glycosylase-like domain superfamily	Homologous Superfamily
A, C, E, G	IPR005122	Uracil-DNA glycosylase-like	Domain
B, D, F, H	IPR024062	Bacteriophage PBS2, uracil-glycosylase inhibitor	Homologous Superfamily
B, D, F, H	IPR043805	Uracil-DNA glycosylase inhibitor	Family

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.