2CG9

Crystal structure of an Hsp90-Sba1 closed chaperone complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000492	biological_process	box C/D snoRNP assembly
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006457	biological_process	protein folding
A	0006458	biological_process	'de novo' protein folding
A	0006626	biological_process	protein targeting to mitochondrion
A	0006970	biological_process	response to osmotic stress
A	0016887	molecular_function	ATP hydrolysis activity
A	0032204	biological_process	regulation of telomere maintenance
A	0032212	biological_process	positive regulation of telomere maintenance via telomerase
A	0032991	cellular_component	protein-containing complex
A	0034605	biological_process	cellular response to heat
A	0042026	biological_process	protein refolding
A	0042802	molecular_function	identical protein binding
A	0043248	biological_process	proteasome assembly
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0050821	biological_process	protein stabilization
A	0051082	molecular_function	unfolded protein binding
A	0051604	biological_process	protein maturation
A	0070482	biological_process	response to oxygen levels
A	0140662	molecular_function	ATP-dependent protein folding chaperone
B	0000166	molecular_function	nucleotide binding
B	0000492	biological_process	box C/D snoRNP assembly
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006457	biological_process	protein folding
B	0006458	biological_process	'de novo' protein folding
B	0006626	biological_process	protein targeting to mitochondrion
B	0006970	biological_process	response to osmotic stress
B	0016887	molecular_function	ATP hydrolysis activity
B	0032204	biological_process	regulation of telomere maintenance
B	0032212	biological_process	positive regulation of telomere maintenance via telomerase
B	0032991	cellular_component	protein-containing complex
B	0034605	biological_process	cellular response to heat
B	0042026	biological_process	protein refolding
B	0042802	molecular_function	identical protein binding
B	0043248	biological_process	proteasome assembly
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0050821	biological_process	protein stabilization
B	0051082	molecular_function	unfolded protein binding
B	0051604	biological_process	protein maturation
B	0070482	biological_process	response to oxygen levels
B	0140662	molecular_function	ATP-dependent protein folding chaperone
X	0051879	molecular_function	Hsp90 protein binding
Y	0051879	molecular_function	Hsp90 protein binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ATP A1678

Chain	Residue
A	GLU33
A	GLY118
A	GLN119
A	GLY121
A	VAL122
A	GLY123
A	PHE124
A	THR171
A	ARG380
A	ASN37
A	ALA38
A	ALA41
A	ASP79
A	MET84
A	ASN92
A	SER99
A	GLY100

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site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE ATP B1678

Chain	Residue
B	GLU33
B	ASN37
B	ASP40
B	ALA41
B	ASP79
B	MET84
B	ASN92
B	SER99
B	GLY100
B	GLY118
B	GLN119
B	PHE120
B	GLY121
B	VAL122
B	GLY123
B	PHE124
B	THR171
B	ARG380

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Functional Information from PROSITE/UniProt

site_id	PS00298
Number of Residues	10
Details	HSP90 Heat shock hsp90 proteins family signature. YsNKEIFLRE

Chain	Residue	Details
A	TYR24-GLU33

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16625188","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2CG9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16625188","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9230303","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AM1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1AMW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CG9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WEP","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P15108","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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