8U1N

Cryo-EM structure of the cross-linked HSP90 dimer (NTD-MD) in the semi-open state

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006457	biological_process	protein folding
A	0016887	molecular_function	ATP hydrolysis activity
A	0032991	cellular_component	protein-containing complex
A	0034605	biological_process	cellular response to heat
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0050821	biological_process	protein stabilization
A	0051082	molecular_function	unfolded protein binding
A	0097718	molecular_function	disordered domain specific binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone
B	0005524	molecular_function	ATP binding
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006457	biological_process	protein folding
B	0016887	molecular_function	ATP hydrolysis activity
B	0032991	cellular_component	protein-containing complex
B	0034605	biological_process	cellular response to heat
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0050821	biological_process	protein stabilization
B	0051082	molecular_function	unfolded protein binding
B	0097718	molecular_function	disordered domain specific binding
B	0140662	molecular_function	ATP-dependent protein folding chaperone

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	TYR33-GLU42

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