2XD6

Hsp90 complexed with a resorcylic acid macrolactone.

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 XD6 A 1215

Chain	Residue
A	ASN37
A	THR171
A	LEU173
A	GOL1216
A	HOH2058
A	HOH2123
A	HOH2124
A	HOH2212
A	HOH2213
A	ASP40
A	ALA41
A	LYS44
A	ASP79
A	ILE82
A	MET84
A	ASN92
A	PHE124

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE GOL A 1216

Chain	Residue
A	ASN37
A	ASP40
A	GLY118
A	GLY121
A	XD61215
A	HOH2061
A	HOH2136
A	HOH2214
A	HOH2215

---

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 1217

Chain	Residue
A	LYS54
A	GLN55
A	THR58
A	ASN141
A	HOH2082

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL A 1218

Chain	Residue
A	ARG32
A	GLU33
A	SER36
A	LEU50
A	HOH2214
A	HOH2216

---

site_id	AC5
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL A 1219

Chain	Residue
A	THR210
A	HOH2103
A	HOH2109

---

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

---

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

---

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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