Annotations: 6Q3Q

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	TPR-like	8079990	3001345	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	TPR-like	8079990	3001345	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	F_UNCLASSIFIED	e6q3qA1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: F_UNCLASSIFIED	ECOD (1.6)
B	F_UNCLASSIFIED	e6q3qB1	A: alpha superhelices	X: Repetitive alpha hairpins	H: ARM repeat (From Topology)	T: ARM repeat	F: F_UNCLASSIFIED	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
C [auth a], D [auth b]	PF00183	Hsp90 protein (HSP90)	Hsp90 protein	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Outer envelope protein 64, mitochondrial	-	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 cellular process establishment of protein localization to mitochondrion 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 cellular process establishment of protein localization to mitochondrion nitrogen compound transport protein transmembrane import into intracellular organelle transport protein import into mitochondrial matrix protein transmembrane transport mitochondrial transport organic substance transport mitochondrial transmembrane transport transmembrane transport import into the mitochondrion protein transport	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle mitochondrial membrane membrane organelle outer membrane organelle envelope bounding membrane of organelle mitochondrial envelope membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle mitochondrial membrane membrane organelle outer membrane organelle envelope bounding membrane of organelle mitochondrial envelope mitochondrial outer membrane outer membrane organelle membrane
C [auth a], D [auth b]	GLY-SER-LYS-MET-GLU-GLU-VAL-ASP	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 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 RNA binding nucleic acid binding mRNA 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 ATP-dependent activity ATP-dependent protein folding chaperone protein folding chaperone	-	membrane-bounded organelle intracellular organelle intracellular anatomical structure Golgi apparatus organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle endomembrane system plastid plastid stroma chloroplast stroma chloroplast extracellular region membrane-bounded organelle intracellular organelle intracellular anatomical structure Golgi apparatus organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle endomembrane system plastid plastid stroma chloroplast stroma chloroplast extracellular region apoplast plant-type vacuole vacuole cell periphery external encapsulating structure plant-type cell wall cell wall

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036928	Amidase signature (AS) superfamily	Homologous Superfamily
A, B	IPR011990	Tetratricopeptide-like helical domain superfamily	Homologous Superfamily
A, B	IPR023631	Amidase signature domain	Domain
A, B	IPR019734	Tetratricopeptide repeat	Repeat
C [auth a], D [auth b]	IPR003594	Histidine kinase/HSP90-like ATPase	Domain
C [auth a], D [auth b]	IPR020575	Heat shock protein Hsp90, N-terminal	Domain
C [auth a], D [auth b]	IPR036890	Histidine kinase/HSP90-like ATPase superfamily	Homologous Superfamily
C [auth a], D [auth b]	IPR037196	HSP90, C-terminal domain	Homologous Superfamily
C [auth a], D [auth b]	IPR020568	Ribosomal protein uS5 domain 2-type superfamily	Homologous Superfamily
C [auth a], D [auth b]	IPR001404	Heat shock protein Hsp90 family	Family
C [auth a], D [auth b]	IPR019805	Heat shock protein Hsp90, conserved site	Conserved Site

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.