Annotations: 5TVU

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00183	e5tvuA2	A: a+b two layers	X: Ribosomal protein S5 domain 2-like (From Topology)	H: Ribosomal protein S5 domain 2-like (From Topology)	T: Ribosomal protein S5 domain 2-like	F: PF00183	ECOD (1.6)
A	PF13589	e5tvuA4	A: a+b two layers	X: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase-like	H: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase (From Topology)	T: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase	F: PF13589	ECOD (1.6)
A	PF00183	e5tvuA3	A: a/b three-layered sandwiches	X: HSP90 C-terminal a/b domain (From Topology)	H: HSP90 C-terminal a/b domain (From Topology)	T: HSP90 C-terminal a/b domain	F: PF00183	ECOD (1.6)
A	PF00183	e5tvuA1	A: mixed a+b and a/b	X: Zincin-like	H: HSP90 C-terminal domain (C-terminal part of Pfam 00183) (From Topology)	T: HSP90 C-terminal domain (C-terminal part of Pfam 00183)	F: PF00183	ECOD (1.6)
B	PF00183	e5tvuB1	A: a+b two layers	X: Ribosomal protein S5 domain 2-like (From Topology)	H: Ribosomal protein S5 domain 2-like (From Topology)	T: Ribosomal protein S5 domain 2-like	F: PF00183	ECOD (1.6)
B	PF13589	e5tvuB4	A: a+b two layers	X: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase-like	H: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase (From Topology)	T: ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase	F: PF13589	ECOD (1.6)
B	PF00183	e5tvuB3	A: a/b three-layered sandwiches	X: HSP90 C-terminal a/b domain (From Topology)	H: HSP90 C-terminal a/b domain (From Topology)	T: HSP90 C-terminal a/b domain	F: PF00183	ECOD (1.6)
B	PF00183	e5tvuB2	A: mixed a+b and a/b	X: Zincin-like	H: HSP90 C-terminal domain (C-terminal part of Pfam 00183) (From Topology)	T: HSP90 C-terminal domain (C-terminal part of Pfam 00183)	F: PF00183	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00183	Hsp90 protein (HSP90)	Hsp90 protein	-	Family
A, B	PF13589	Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase (HATPase_c_3)	Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase	This family represents, additionally, the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	TNF receptor-associated protein 1	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding calcium ion binding unfolded protein binding protein binding kinase binding enzyme binding protein kinase binding 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 catalytic activity ATP-dependent activity ATP-dependent protein folding chaperone protein folding chaperone identical protein binding	nucleobase-containing compound metabolic process organic cyclic compound metabolic process organic substance metabolic process metabolic process primary metabolic process macromolecule metabolic process nucleic acid metabolic process organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process gene expression macromolecule biosynthetic process protein maturation protein folding nucleobase-containing compound metabolic process organic cyclic compound metabolic process organic substance metabolic process metabolic process primary metabolic process macromolecule metabolic process nucleic acid metabolic process organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process gene expression macromolecule biosynthetic process protein maturation protein folding biosynthetic process organic substance biosynthetic process cellular process protein metabolic process	membrane-bounded organelle mitochondrial membrane intracellular anatomical structure organelle inner membrane mitochondrion membrane cellular anatomical entity intracellular membrane-bounded organelle mitochondrial inner membrane intracellular organelle organelle envelope mitochondrial envelope organelle cytoplasm membrane-bounded organelle mitochondrial membrane intracellular anatomical structure organelle inner membrane mitochondrion membrane cellular anatomical entity intracellular membrane-bounded organelle mitochondrial inner membrane intracellular organelle organelle envelope mitochondrial envelope organelle cytoplasm organelle membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR003594	Histidine kinase/HSP90-like ATPase	Domain
A, B	IPR020575	Heat shock protein Hsp90, N-terminal	Domain
A, B	IPR036890	Histidine kinase/HSP90-like ATPase superfamily	Homologous Superfamily
A, B	IPR037196	HSP90, C-terminal domain	Homologous Superfamily
A, B	IPR020568	Ribosomal protein uS5 domain 2-type superfamily	Homologous Superfamily
A, B	IPR001404	Heat shock protein Hsp90 family	Family

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.