2YGF

L89V, L93I and V136M Mutant of N-Term HSP90 complexed with Geldanamycin

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	23
Details	BINDING SITE FOR RESIDUE GDM A 1215

Chain	Residue
A	ASN37
A	GLY121
A	VAL122
A	GLY123
A	PHE124
A	MET136
A	THR171
A	HOH2032
A	HOH2033
A	HOH2035
A	HOH2072
A	ALA38
A	HOH2087
A	HOH2100
A	HOH2146
A	HOH2147
A	ASP40
A	ALA41
A	LYS44
A	ASP79
A	ILE82
A	ASN92
A	LYS98

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site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1216

Chain	Residue
A	ARG65
A	LYS69
A	GLU71
A	THR210
A	HOH2062
A	HOH2148

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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	TYR24-GLU33

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16625188","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2CG9","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16625188","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9230303","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AM1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1AMW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2CG9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WEP","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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