2WEQ

Yeast Hsp90 N-terminal domain LI-IV mutant 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	20
Details	BINDING SITE FOR RESIDUE GDM A 1215

Chain	Residue
A	ASN37
A	GLY121
A	VAL122
A	GLY123
A	PHE124
A	TYR125
A	THR171
A	HOH2021
A	HOH2024
A	HOH2044
A	HOH2110
A	ASP40
A	HOH2112
A	LYS44
A	ASP79
A	ILE82
A	MET84
A	ASN92
A	LEU93
A	LYS98

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

Chain	Residue
A	ARG32
A	GLU33
A	SER36
A	GLY118
A	HOH2014
A	HOH2113

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site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1217

Chain	Residue
A	GLU187
A	VAL209
A	LYS211
A	LYS211
A	HOH2114
A	HOH2115

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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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