3N72

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF09229	e3n72A1	A: a+b complex topology	X: Aha1/BPI domain-like (From Topology)	H: Aha1/BPI domain-like (From Topology)	T: Aha1/BPI domain-like	F: PF09229	ECOD (1.6)
B	PF09229	e3n72B1	A: a+b complex topology	X: Aha1/BPI domain-like (From Topology)	H: Aha1/BPI domain-like (From Topology)	T: Aha1/BPI domain-like	F: PF09229	ECOD (1.6)

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.15.10.20	Alpha Beta	Super Roll	Bactericidal permeability-increasing protein	domain 1	CATH (4.3.0)
B	3.15.10.20	Alpha Beta	Super Roll	Bactericidal permeability-increasing protein	domain 1	CATH (4.3.0)

Chains	Accession	Name	Description	Comments	Source
A, B	PF09229	Activator of Hsp90 ATPase, N-terminal (Aha1_N)	Activator of Hsp90 ATPase, N-terminal	Members of this family, which are predominantly found in the protein 'Activator of Hsp90 ATPase' adopt a secondary structure consisting of an N-terminal alpha-helix leading into a four-stranded meandering antiparallel beta-sheet, followed by a C-term ...	Members of this family, which are predominantly found in the protein 'Activator of Hsp90 ATPase' adopt a secondary structure consisting of an N-terminal alpha-helix leading into a four-stranded meandering antiparallel beta-sheet, followed by a C-terminal alpha-helix. The two helices are packed together, with the beta-sheet curving around them. They bind to the molecular chaperone HSP82 and stimulate its ATPase activity [1].	Domain

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	putative activator of HSP90	ATPase activator activity molecular function activator activity molecular function regulator activity ATPase regulator activity protein binding binding protein-folding chaperone binding	-	-