5LNY

HSP90 WITH indazole derivative

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005524	molecular_function	ATP binding
A	0006457	biological_process	protein folding
A	0016887	molecular_function	ATP hydrolysis activity
A	0051082	molecular_function	unfolded protein binding
A	0140662	molecular_function	ATP-dependent protein folding chaperone

Functional Information from PDB Data

site_id	AC1
Number of Residues	16
Details	binding site for residue 70K A 301

Chain	Residue
A	ASN51
A	PHE138
A	THR184
A	VAL186
A	HOH444
A	HOH480
A	HOH507
A	HOH573
A	ASP54
A	ALA55
A	ASP93
A	ILE96
A	GLY97
A	MET98
A	LEU107
A	GLY135

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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	TYR38-GLU47

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	BINDING:

Chain	Residue	Details
A	GLU16

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:2492519, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	THR109

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	MET130

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000269|PubMed:2492519, ECO:0007744|PubMed:16807684, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	ALA141

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P07901

Chain	Residue	Details
A	LYS191

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