6AOM

Structure of molecular chaperone Grp94 bound to selective inhibitor methyl 2-[2-(2-benzylphenyl)ethyl]-3-chloro-4,6-dihydroxybenzoate

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
B	0005524	molecular_function	ATP binding
B	0006457	biological_process	protein folding
B	0016887	molecular_function	ATP hydrolysis activity
B	0051082	molecular_function	unfolded protein binding
B	0140662	molecular_function	ATP-dependent protein folding chaperone

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue P33 A 401

Chain	Residue
A	GLU131
A	TYR280

---

site_id	AC2
Number of Residues	3
Details	binding site for residue P33 A 402

Chain	Residue
A	LYS137
A	THR148
A	P33403

---

site_id	AC3
Number of Residues	6
Details	binding site for residue P33 A 403

Chain	Residue
B	LEU117
B	THR121
A	THR212
A	ARG237
A	THR248
A	P33402

---

site_id	AC4
Number of Residues	6
Details	binding site for residue P33 A 404

Chain	Residue
A	LEU117
A	THR121
B	THR212
B	ARG237
B	THR248
B	P33408

---

site_id	AC5
Number of Residues	3
Details	binding site for residue P33 A 405

Chain	Residue
A	ASN216
A	ASP218
B	ASP262

---

site_id	AC6
Number of Residues	5
Details	binding site for residue P33 A 406

Chain	Residue
A	ARG156
A	ASP218
A	THR219
A	HIS221
B	THR263

---

site_id	AC7
Number of Residues	4
Details	binding site for residue P33 A 407

Chain	Residue
A	ASN83
A	LYS87
A	LEU88
A	SER227

---

site_id	AC8
Number of Residues	1
Details	binding site for residue P33 A 408

Chain	Residue
A	ARG84

---

site_id	AC9
Number of Residues	18
Details	binding site for residue VC5 A 409

Chain	Residue
A	LEU104
A	ASN107
A	ASP110
A	ALA111
A	LYS114
A	ASP149
A	GLY153
A	MET154
A	ASN162
A	LEU163
A	GLY196
A	VAL197
A	PHE199
A	TYR200
A	THR245
A	ILE247
A	HOH501
A	HOH503

---

site_id	AD1
Number of Residues	5
Details	binding site for residue GOL A 410

Chain	Residue
A	LYS75
A	GLU224
A	ASP226
A	GLU229
A	SER231

---

site_id	AD2
Number of Residues	3
Details	binding site for residue P33 B 401

Chain	Residue
A	THR263
A	ASN266
B	LYS214

---

site_id	AD3
Number of Residues	4
Details	binding site for residue P33 B 402

Chain	Residue
B	GLU103
B	SER106
B	ASP110
B	GLY193

---

site_id	AD4
Number of Residues	3
Details	binding site for residue P33 B 403

Chain	Residue
B	GLU131
B	TYR280
B	TRP333

---

site_id	AD5
Number of Residues	1
Details	binding site for residue PEG B 404

Chain	Residue
B	LYS137

---

site_id	AD6
Number of Residues	2
Details	binding site for residue P33 B 405

Chain	Residue
B	ASP110
B	ASP113

---

site_id	AD7
Number of Residues	1
Details	binding site for residue P33 B 406

Chain	Residue
B	ASN337

---

site_id	AD8
Number of Residues	2
Details	binding site for residue P33 B 407

Chain	Residue
B	ASN124
B	ASN216

---

site_id	AD9
Number of Residues	2
Details	binding site for residue P33 B 408

Chain	Residue
A	P33404
B	LYS137

---

site_id	AE1
Number of Residues	15
Details	binding site for residue VC5 B 409

Chain	Residue
B	LEU104
B	ASN107
B	ASP110
B	ALA111
B	ASP149
B	GLY153
B	MET154
B	ASN162
B	GLY196
B	VAL197
B	PHE199
B	TYR200
B	THR245
B	ILE247
B	HOH501

---

Functional Information from PROSITE/UniProt

site_id	PS00298
Number of Residues	10
Details	HSP90 Heat shock hsp90 proteins family signature. YkNKEIFLRE

Chain	Residue	Details
A	TYR94-GLU103

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15292259","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15951571","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17936703","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TC0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TC6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YT0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O1U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O1V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15292259","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15951571","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17936703","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TBW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TC0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TC6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1YT0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O1U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O1V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"15292259","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15951571","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17936703","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TBW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TC0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1TC6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O1U","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2O1V","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P14625","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q66HD0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---