5FNF

Dynamic Undocking and the Quasi-Bound State as tools for Drug Design

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	2
Details	BINDING SITE FOR RESIDUE SO4 A 1224

Chain	Residue
A	PHE138
A	TRP162

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site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 1225

Chain	Residue
A	HIS77
A	ASN79

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site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE TQL A 1226

Chain	Residue
A	THR184
A	VAL186
A	HOH2032
A	HOH2034
A	HOH2082
A	ASN51
A	ALA55
A	ASP93
A	ILE96
A	GLY97

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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 site: {}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	1
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07901","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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