4ZO0 | pdb_00004zo0

X-ray Structure of AAV-2 Origin Binding Domain

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	d4zo0a_	Alpha and beta proteins (a+b)	Origin of replication-binding domain, RBD-like	Origin of replication-binding domain, RBD-like	Replication protein Rep, nuclease domain	automated matches	AAV-2 (Adeno-associated virus 2 Srivastava/1982 ) [TaxId: 648242 ],	SCOPe (2.08)
B	d4zo0b_	Alpha and beta proteins (a+b)	Origin of replication-binding domain, RBD-like	Origin of replication-binding domain, RBD-like	Replication protein Rep, nuclease domain	automated matches	AAV-2 (Adeno-associated virus 2 Srivastava/1982 ) [TaxId: 648242 ],	SCOPe (2.08)
C	d4zo0c1	Alpha and beta proteins (a+b)	Origin of replication-binding domain, RBD-like	Origin of replication-binding domain, RBD-like	Replication protein Rep, nuclease domain	automated matches	AAV-2 (Adeno-associated virus 2 Srivastava/1982 ) [TaxId: 648242 ],	SCOPe (2.08)
C	d4zo0c2	Artifacts	Tags	Tags	Tags	N-terminal Tags	AAV-2 (Adeno-associated virus 2 Srivastava/1982 ) [TaxId: 648242 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Origin of replication-binding domain, RBD-like	8089616	3001937	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Origin of replication-binding domain, RBD-like	8089616	3001937	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Origin of replication-binding domain, RBD-like	8089616	3001937	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	Rep_N	e4zo0A1	A: a+b two layers	X: Alpha-beta plaits	H: Origin of replication-binding domains	T: Origin of replication-binding domains	F: Rep_N	ECOD (1.6)
B	Rep_N	e4zo0B1	A: a+b two layers	X: Alpha-beta plaits	H: Origin of replication-binding domains	T: Origin of replication-binding domains	F: Rep_N	ECOD (1.6)
C	Rep_N	e4zo0C1	A: a+b two layers	X: Alpha-beta plaits	H: Origin of replication-binding domains	T: Origin of replication-binding domains	F: Rep_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.1310.20	Alpha Beta	3-Layer(aba) Sandwich	Replication Protein E1	Chain: A,	CATH (4.3.0)
B	3.40.1310.20	Alpha Beta	3-Layer(aba) Sandwich	Replication Protein E1	Chain: A,	CATH (4.3.0)
C	3.40.1310.20	Alpha Beta	3-Layer(aba) Sandwich	Replication Protein E1	Chain: A,	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF08724	Rep protein catalytic domain like (Rep_N)	Rep protein catalytic domain like	Adeno-associated virus (AAV) Replication (Rep) protein is essential for viral replication and integration. The catalytic domain has DNA binding and endonuclease activity.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	Protein Rep68	ATP-dependent activity, acting on DNA catalytic activity, acting on DNA DNA translocase activity catalytic activity, acting on a nucleic acid chromatin extrusion motor activity catalytic activity ATP-dependent activity ATP-dependent H3-H4 histone complex chaperone activity catalytic activity, acting on a protein histone chaperone activity ATP-dependent chromatin remodeler activity H3-H4 histone complex chaperone activity protein carrier chaperone ATP-dependent histone chaperone activity ATP-dependent activity, acting on DNA catalytic activity, acting on DNA DNA translocase activity catalytic activity, acting on a nucleic acid chromatin extrusion motor activity catalytic activity ATP-dependent activity ATP-dependent H3-H4 histone complex chaperone activity catalytic activity, acting on a protein histone chaperone activity ATP-dependent chromatin remodeler activity H3-H4 histone complex chaperone activity protein carrier chaperone ATP-dependent histone chaperone activity molecular carrier activity cohesin loader activity DNA clamp loader activity ATP-dependent H2AZ histone chaperone activity nucleic acid conformation isomerase activity forked DNA-dependent helicase activity isomerase activity DNA helicase activity helicase activity macromolecular conformation isomerase activity binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding DNA binding nucleic acid binding single-stranded DNA helicase activity 3'-5' DNA helicase activity single-stranded 3'-5' DNA helicase activity four-way junction helicase activity pyrophosphatase activity ATP hydrolysis activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides endonuclease activity nuclease activity hydrolase activity, acting on ester bonds cation binding metal ion binding double-stranded DNA helicase activity	nucleobase-containing compound metabolic process DNA replication metabolic process cellular process primary metabolic process DNA metabolic process macromolecule metabolic process nucleic acid metabolic process viral DNA genome replication viral life cycle nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid biosynthetic process biosynthetic process nucleobase-containing compound metabolic process DNA replication metabolic process cellular process primary metabolic process DNA metabolic process macromolecule metabolic process nucleic acid metabolic process viral DNA genome replication viral life cycle nucleobase-containing compound biosynthetic process macromolecule biosynthetic process nucleic acid biosynthetic process biosynthetic process viral genome replication viral process DNA biosynthetic process symbiont-mediated perturbation of host cellular process biological process involved in interspecies interaction between organisms symbiont-mediated perturbation of host process symbiont-mediated perturbation of host cell cycle progression symbiont-mediated arrest of host cell cycle during G2/M transition modulation of process of another organism biological process involved in interaction with host biological process involved in symbiotic interaction symbiont-mediated disruption of host anatomical structure symbiont entry into host cell via permeabilization of host membrane symbiont-mediated disruption of host cellular anatomical structure symbiont-mediated perturbation of host membrane symbiont entry into host cell symbiont entry into host disruption of anatomical structure in another organism symbiont-mediated perturbation of host cell cycle G1/S transition checkpoint	host intracellular membrane-bounded organelle host cellular component host intracellular part cellular anatomical structure host cell part host intracellular region host cell nucleus host intracellular organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR014835	NS1 nuclease, NS1-Nuc domain, parvovirinae	Domain
A, B, C	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
A, B, C	IPR014015	Helicase, superfamily 3, DNA virus	Domain
A, B, C	IPR049901	NS1 nuclease, NS1-Nuc domain, Parvovirus	Domain
A, B, C	IPR001257	Parvovirus non-structural protein 1, helicase domain	Domain

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.