1UYD

Human Hsp90-alpha with 9-Butyl-8-(2-chloro-3,4,5-trimethoxy-benzyl)-9H-purin-6-ylamine

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 PU8 A1224

Chain	Residue
A	ASN51
A	TYR139
A	TRP162
A	THR184
A	HOH2177
A	HOH2275
A	HOH2276
A	HOH2277
A	SER52
A	ALA55
A	ASP93
A	MET98
A	LEU103
A	LEU107
A	ALA111
A	PHE138

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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	3
Details	BINDING:

Chain	Residue	Details
A	SER52
A	THR94
A	TYR139

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	SER113

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by PRKDC => ECO:0000269|PubMed:2507541

Chain	Residue	Details
A	GLN8
A	GLN6

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site_id	SWS_FT_FI4
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P07901

Chain	Residue	Details
A	ILE59
A	GLN85

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site_id	SWS_FT_FI5
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	ASP232

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