5K83

Crystal Structure of a Primate APOBEC3G N-Domain, in Complex with ssDNA

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth D]	SCOP2B Superfamily	Cytidine deaminase-like	8105528	3001838	SCOP2B (2022-06-29)
B [auth C]	SCOP2B Superfamily	Cytidine deaminase-like	8105528	3001838	SCOP2B (2022-06-29)
D [auth F]	SCOP2B Superfamily	Cytidine deaminase-like	8105528	3001838	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	Cytidine deaminase-like	8105528	3001838	SCOP2B (2022-06-29)
G [auth B]	SCOP2B Superfamily	Cytidine deaminase-like	8105528	3001838	SCOP2B (2022-06-29)
H [auth A]	SCOP2B Superfamily	Cytidine deaminase-like	8105528	3001838	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 [auth D]	PF18782	e5k83D1	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: PF18782	ECOD (1.6)
B [auth C]	PF18782	e5k83C1	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: PF18782	ECOD (1.6)
D [auth F]	PF18782	e5k83F1	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: PF18782	ECOD (1.6)
E	PF18782	e5k83E1	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: PF18782	ECOD (1.6)
G [auth B]	PF18782	e5k83B1	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: PF18782	ECOD (1.6)
H [auth A]	PF18782	e5k83A1	A: a+b three layers	X: Cytidine deaminase-like (From Topology)	H: Cytidine deaminase-like (From Topology)	T: Cytidine deaminase-like	F: PF18782	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth D], B [auth C], D [auth F], E, G [auth B], A [auth D], B [auth C], D [auth F], E, G [auth B], H [auth A]	PF18782	Novel AID APOBEC clade 2 (NAD2)	Novel AID APOBEC clade 2	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth D], B [auth C], D [auth F], E, G [auth B], A [auth D], B [auth C], D [auth F], E, G [auth B], H [auth A]	Apolipoprotein B mRNA editing enzyme, catalytic peptide-like 3G,Apolipoprotein B mRNA editing enzyme, catalytic peptide-like 3G	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines deoxycytidine deaminase activity hydrolase activity catalytic activity deaminase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds cytidine deaminase activity cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding	DNA cytosine deamination primary metabolic process DNA metabolic process nucleic acid metabolic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process DNA deamination DNA modification organic substance metabolic process macromolecule modification metabolic process macromolecule metabolic process regulation of biological process regulation of cellular process DNA cytosine deamination primary metabolic process DNA metabolic process nucleic acid metabolic process nucleobase-containing compound metabolic process organic cyclic compound metabolic process DNA deamination DNA modification organic substance metabolic process macromolecule modification metabolic process macromolecule metabolic process regulation of biological process regulation of cellular process negative regulation of cellular process biological regulation negative regulation of biological process cellular process retrotransposon silencing transposition retrotransposition biological process involved in interspecies interaction between organisms response to stimulus immune response response to other organism defense response defense response to symbiont response to external stimulus response to biotic stimulus immune system process defense response to other organism response to stress innate immune response response to external biotic stimulus defense response to virus response to virus	intracellular anatomical structure cytoplasmic ribonucleoprotein granule cellular anatomical entity ribonucleoprotein granule intracellular organelle organelle intracellular non-membrane-bounded organelle cytoplasm supramolecular complex P-body non-membrane-bounded organelle protein-containing complex ribonucleoprotein complex membrane-bounded organelle intracellular anatomical structure cytoplasmic ribonucleoprotein granule cellular anatomical entity ribonucleoprotein granule intracellular organelle organelle intracellular non-membrane-bounded organelle cytoplasm supramolecular complex P-body non-membrane-bounded organelle protein-containing complex ribonucleoprotein complex membrane-bounded organelle nucleus intracellular membrane-bounded organelle
C [auth I], F [auth J], I [auth H]	DNA (5'-D(TPTPTPTPTPTPTPTPTPT)-3')	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth D], B [auth C], D [auth F], E, G [auth B], A [auth D], B [auth C], D [auth F], E, G [auth B], H [auth A]	IPR016193	Cytidine deaminase-like	Homologous Superfamily
A [auth D], B [auth C], D [auth F], E, G [auth B], A [auth D], B [auth C], D [auth F], E, G [auth B], H [auth A]	IPR002125	Cytidine and deoxycytidylate deaminase domain	Domain
A [auth D], B [auth C], D [auth F], E, G [auth B], A [auth D], B [auth C], D [auth F], E, G [auth B], H [auth A]	IPR016192	APOBEC/CMP deaminase, zinc-binding	Binding Site

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 R01GM133198.