1U0Z

N-Domain Of Grp94 Lacking The Charged Domain In Complex With Radicicol

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	17
Details	BINDING SITE FOR RESIDUE RDC A 301

Chain	Residue
A	LEU104
A	PHE199
A	THR245
A	ILE247
A	PG4403
A	HOH413
A	HOH415
A	HOH458
A	HOH532
A	ASN107
A	ASP110
A	ALA111
A	LYS114
A	ASP149
A	MET154
A	ASN162
A	LEU163

---

site_id	AC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PG4 A 401

Chain	Residue
A	THR212
A	ARG237
A	THR240
A	THR248
A	PG4402
A	HOH488
A	HOH509
A	HOH511
A	HOH538

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PG4 A 402

Chain	Residue
A	LYS137
A	THR148
A	THR246
A	TRP282
A	PG4401
A	HOH516

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PG4 A 403

Chain	Residue
A	ASP110
A	ASP113
A	LYS114
A	LEU117
A	RDC301
A	HOH507

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PG4 A 404

Chain	Residue
A	LYS75
A	PHE76
A	ALA77
A	HOH455

---

site_id	AC6
Number of Residues	16
Details	BINDING SITE FOR RESIDUE RDC B 302

Chain	Residue
B	LEU104
B	ASN107
B	ASP110
B	ALA111
B	LYS114
B	ASP149
B	MET154
B	ASN162
B	LEU163
B	PHE199
B	THR245
B	ILE247
B	PG4410
B	HOH413
B	HOH423
B	HOH529

---

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PG4 B 405

Chain	Residue
B	ILE210
B	THR212
B	ARG237
B	THR248
B	HOH456
B	HOH487

---

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PG4 B 406

Chain	Residue
B	LYS137
B	THR148
B	TRP282
B	TRP333
B	HOH501

---

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PG4 B 407

Chain	Residue
B	ASN129
B	ASN239
B	GLY242
B	HOH530

---

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PG4 B 408

Chain	Residue
B	ASP262
B	THR263
B	ASN266
B	HOH507
B	HOH527
B	HOH545

---

site_id	BC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE 1PE A 409

Chain	Residue
A	ASN83
A	LYS87
A	ILE90
A	SER227
A	HOH479
B	ASN83
B	MET86
B	LYS87
B	ILE90
B	SER227

---

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE PG4 B 410

Chain	Residue
B	LYS114
B	RDC302
B	HOH537
B	HOH548

---

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

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"UniProtKB","id":"P14625","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---