1ZWH

Yeast Hsp82 in complex with the novel Hsp90 inhibitor Radester amine

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	d1zwha2	Alpha and beta proteins (a+b)	ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase	ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase	Heat shock protein 90, HSP90, N-terminal domain	HSP90	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
A	d1zwha3	Artifacts	Tags	Tags	Tags	N-terminal Tags	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	GHKL (Gyrase, Hsp90, Histidine Kinase, MutL) domain-like	8042891	3000091	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	HATPase_c	e1zwhA1	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: HATPase_c	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.565.10	Alpha Beta	2-Layer Sandwich	Heat Shock Protein 90	Histidine kinase-like ATPase, C-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF02518	Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase (HATPase_c)	Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase	This family represents 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	ATP-dependent molecular chaperone HSP82	ATP-dependent protein folding chaperone protein folding chaperone ATP-dependent activity binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP-dependent protein folding chaperone protein folding chaperone ATP-dependent activity binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding unfolded protein binding protein 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 identical protein binding	protein refolding primary metabolic process gene expression macromolecule biosynthetic process protein maturation protein folding biosynthetic process metabolic process cellular process protein metabolic process macromolecule metabolic process protein localization establishment of protein localization cellular localization protein refolding primary metabolic process gene expression macromolecule biosynthetic process protein maturation protein folding biosynthetic process metabolic process cellular process protein metabolic process macromolecule metabolic process protein localization establishment of protein localization cellular localization protein targeting establishment of localization localization establishment of protein localization to organelle cellular macromolecule localization macromolecule localization protein localization to organelle protein localization to mitochondrion protein targeting to mitochondrion establishment of protein localization to mitochondrion regulation of protein stability biological regulation regulation of biological quality protein stabilization cellular response to stimulus cellular response to heat response to stimulus cellular response to stress response to stress response to heat response to abiotic stimulus response to temperature stimulus cellular component organization cellular component biogenesis proteasome assembly cellular component assembly protein-containing complex organization protein-containing complex assembly cellular component organization or biogenesis response to oxygen levels regulation of telomere maintenance regulation of cellular component organization regulation of cellular process telomere organization regulation of primary metabolic process nucleobase-containing compound metabolic process regulation of nucleobase-containing compound metabolic process regulation of biological process chromosome organization regulation of chromosome organization regulation of macromolecule metabolic process DNA metabolic process regulation of organelle organization nucleic acid metabolic process telomere maintenance organelle organization regulation of metabolic process regulation of DNA metabolic process ribonucleoprotein complex biogenesis small nucleolar ribonucleoprotein complex assembly protein-RNA complex assembly protein-RNA complex organization box C/D snoRNP assembly positive regulation of organelle organization regulation of DNA biosynthetic process positive regulation of macromolecule biosynthetic process RNA-templated DNA biosynthetic process telomere maintenance via telomere lengthening positive regulation of metabolic process positive regulation of telomere maintenance via telomere lengthening positive regulation of macromolecule metabolic process positive regulation of telomere maintenance positive regulation of nucleobase-containing compound metabolic process regulation of telomere maintenance via telomere lengthening positive regulation of chromosome organization positive regulation of DNA metabolic process positive regulation of telomere maintenance via telomerase regulation of macromolecule biosynthetic process DNA biosynthetic process positive regulation of cellular component organization positive regulation of biological process nucleic acid biosynthetic process positive regulation of biosynthetic process positive regulation of cellular process regulation of biosynthetic process telomere maintenance via telomerase positive regulation of DNA biosynthetic process nucleobase-containing compound biosynthetic process regulation of telomere maintenance via telomerase 'de novo' protein folding response to osmotic stress	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol cell periphery plasma membrane membrane protein-containing complex perinuclear region of cytoplasm membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR020575	Heat shock protein Hsp90, N-terminal	Domain
A	IPR036890	Histidine kinase/HSP90-like ATPase superfamily	Homologous Superfamily
A	IPR037196	HSP90, C-terminal domain	Homologous Superfamily
A	IPR003594	Histidine kinase/HSP90-like ATPase domain	Domain
A	IPR020568	Ribosomal protein uS5 domain 2-type superfamily	Homologous Superfamily
A	IPR001404	Heat shock protein Hsp90 family	Family
A	IPR019805	Heat shock protein Hsp90, conserved site	Conserved 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 R01GM157729.