1A4H

STRUCTURE OF THE N-TERMINAL DOMAIN OF THE YEAST HSP90 CHAPERONE IN COMPLEX 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	17
Details	BINDING SITE FOR RESIDUE GDM A 300

Chain	Residue
A	ASN37
A	LYS98
A	GLY121
A	VAL122
A	GLY123
A	PHE124
A	THR171
A	HOH400
A	HOH529
A	ASP40
A	ALA41
A	LYS44
A	ASP79
A	ILE82
A	MET84
A	ASN92
A	LEU93

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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: BINDING => ECO:0000269|PubMed:16625188, ECO:0007744|PDB:2CG9

Chain	Residue	Details
A	GLU33
A	MET84
A	ASN92
A	LYS98
A	SER99
A	THR171

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:16625188, ECO:0000269|PubMed:9230303, ECO:0007744|PDB:1AM1, ECO:0007744|PDB:1AMW, ECO:0007744|PDB:2CG9, ECO:0007744|PDB:2WEP

Chain	Residue	Details
A	ASN37
A	ASP79
A	GLN119

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