3C11

Yeast Hsp82 N-terminal domain-Geldanamycin complex: effects of mutants 98-99 KS-AA

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 300

Chain	Residue
A	ASN37
A	GLY121
A	VAL122
A	GLY123
A	PHE124
A	THR171
A	HOH402
A	HOH403
A	HOH406
A	HOH407
A	HOH439
A	ASP40
A	HOH465
A	HOH512
A	HOH525
A	HOH564
A	ALA41
A	LYS44
A	ASP79
A	ILE82
A	MET84
A	ASN92
A	LEU93

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 301

Chain	Residue
A	LYS54
A	GLN55
A	THR58

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site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 302

Chain	Residue
A	THR58
A	GLU59
A	ARG78
A	GLY168
A	HOH495
A	HOH587
A	HOH599

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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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