3MNR

Crystal Structure of Benzamide SNX-1321 bound to Hsp90

Functional Information from GO Data

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE SD1 P 233

Chain	Residue
P	ASN51
P	TRP162
P	THR184
P	HOH263
P	HOH283
P	HOH458
P	HOH562
P	ALA55
P	LYS58
P	TYR61
P	ASP93
P	GLY97
P	MET98
P	ASP102
P	TYR139

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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
P	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
P	ASN51
P	ASP93
P	PHE138

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

Chain	Residue	Details
P	LYS112

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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
P	THR5
P	THR7

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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
P	LYS58
P	LYS84

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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
P	SER231

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