1AM1

ATP BINDING SITE IN THE HSP90 MOLECULAR CHAPERONE

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	20
Details	BINDING SITE FOR RESIDUE ADP A 300

Chain	Residue
A	ASN92
A	LEU93
A	LYS98
A	GLY121
A	VAL122
A	GLY123
A	PHE124
A	THR171
A	HOH400
A	HOH403
A	HOH404
A	HOH408
A	HOH624
A	HOH625
A	HOH626
A	HOH628
A	ASN37
A	ALA41
A	ASP79
A	MET84

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site_id	S1
Number of Residues	5
Details	ATP BINDING SITE.

Chain	Residue
A	ASP79
A	ASN92
A	ASN37
A	PHE124
A	LYS98

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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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