5OXF

An oligomerised bacterial dynamin pair provides a mechanism for the long range sensing and tethering of membranes

External Resource: Annotation

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

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	F_UNCLASSIFIED	e5oxfA3	A: alpha arrays	X: Assembly domain of GTP-binding protein (From Topology)	H: Assembly domain of GTP-binding protein (From Topology)	T: Assembly domain of GTP-binding protein	F: F_UNCLASSIFIED	ECOD (1.6)
A	F_UNCLASSIFIED	e5oxfA2	A: alpha bundles	X: Bacterial dynamin-like protein helical domain (From Topology)	H: Bacterial dynamin-like protein helical domain (From Topology)	T: Bacterial dynamin-like protein helical domain	F: F_UNCLASSIFIED	ECOD (1.6)
A	PF00350	e5oxfA1	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF00350	ECOD (1.6)
C	F_UNCLASSIFIED	e5oxfC2	A: alpha bundles	X: Bacterial dynamin-like protein helical domain (From Topology)	H: Bacterial dynamin-like protein helical domain (From Topology)	T: Bacterial dynamin-like protein helical domain	F: F_UNCLASSIFIED	ECOD (1.6)
C	PF00350	e5oxfC1	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF00350	ECOD (1.6)
D	F_UNCLASSIFIED	e5oxfD2	A: alpha bundles	X: Bacterial dynamin-like protein helical domain (From Topology)	H: Bacterial dynamin-like protein helical domain (From Topology)	T: Bacterial dynamin-like protein helical domain	F: F_UNCLASSIFIED	ECOD (1.6)
D	PF00350	e5oxfD1	A: a/b three-layered sandwiches	X: P-loop domains-like	H: P-loop domains-related	T: P-loop containing nucleoside triphosphate hydrolases	F: PF00350	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00350	Dynamin family (Dynamin_N)	Dynamin family	-	Domain
C, D	PF00350	Dynamin family (Dynamin_N)	Dynamin family	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	GTP-binding protein	binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding organic cyclic compound binding purine nucleotide binding anion binding heterocyclic compound binding carbohydrate derivative binding binding guanyl nucleotide binding GTP binding nucleotide binding guanyl ribonucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding organic cyclic compound binding purine nucleotide binding anion binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding pyrophosphatase activity GTPase activity ribonucleoside triphosphate phosphatase activity hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides hydrolase activity hydrolase activity, acting on acid anhydrides catalytic activity	-	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol
C, D	GTP-binding protein	hydrolase activity catalytic activity	-	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR045063	Dynamin, N-terminal	Domain
A, B	IPR030381	Dynamin-type guanine nucleotide-binding (G) domain	Domain
A, B	IPR027094	Mitofusin family	Family
A, B	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily
C, D	IPR045063	Dynamin, N-terminal	Domain
C, D	IPR022812	Dynamin	Family
C, D	IPR027417	P-loop containing nucleoside triphosphate hydrolase	Homologous Superfamily

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.