5FND

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	13
Details	BINDING SITE FOR RESIDUE IQ5 A 1225

Chain	Residue
A	ALA55
A	THR184
A	HOH2064
A	HOH2065
A	HOH2106
A	LYS58
A	ASP93
A	ILE96
A	GLY97
A	MET98
A	ASP102
A	LEU107
A	GLY108

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 1226

Chain	Residue
A	GLU75
A	HIS77
A	ASN79
A	HOH2197

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 1227

Chain	Residue
A	ASP54
A	ASP54

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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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