5Y3N

Structure of TRAP1 complexed with DN401

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	11
Details	binding site for residue 8MF A 601

Chain	Residue
A	ALA123
A	HOH720
A	HOH726
A	ASP158
A	ILE161
A	GLY162
A	MET163
A	PHE201
A	PHE205
A	TRP231
A	THR251

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	5
Details	BINDING: BINDING => ECO:0000250

Chain	Residue	Details
A	ASN119
A	ASP158
A	ASN171
A	PHE205
A	ARG402

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site_id	SWS_FT_FI2
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q5XHZ0

Chain	Residue	Details
A	SER170

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site_id	SWS_FT_FI3
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q5XHZ0

Chain	Residue	Details
A	THR174

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER194

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site_id	SWS_FT_FI5
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9CQN1

Chain	Residue	Details
A	LYS262
A	LYS324
A	LYS431

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site_id	SWS_FT_FI6
Number of Residues	3
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS332
A	LYS424
A	LYS466

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site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648

Chain	Residue	Details
A	THR494

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