6C91

Structure of GRP94 with a resorcinylic inhibitor.

Functional Information from GO Data

Chain	GOid	namespace	contents
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
C	0005524	molecular_function	ATP binding
C	0006457	biological_process	protein folding
C	0016887	molecular_function	ATP hydrolysis activity
C	0051082	molecular_function	unfolded protein binding
C	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 SO4 C 401

Chain	Residue
C	LYS135
C	TRP333

---

site_id	AC2
Number of Residues	2
Details	binding site for residue SO4 C 402

Chain	Residue
C	LYS214
C	ASN217

---

site_id	AC3
Number of Residues	10
Details	binding site for residue EQD C 403

Chain	Residue
C	THR245
C	ILE247
C	HOH502
C	HOH503
C	HOH510
C	ALA111
C	ASP149
C	MET154
C	ASN162
C	PHE195

---

site_id	AC4
Number of Residues	5
Details	binding site for residue EDO C 404

Chain	Residue
B	VAL250
C	THR219
C	GLN220
C	ASP235
C	GLY238

---

site_id	AC5
Number of Residues	3
Details	binding site for residue EDO C 405

Chain	Residue
B	EDO408
C	EDO406
C	HOH504

---

site_id	AC6
Number of Residues	3
Details	binding site for residue EDO C 406

Chain	Residue
C	ASN96
C	TYR271
C	EDO405

---

site_id	AC7
Number of Residues	4
Details	binding site for residue SO4 B 401

Chain	Residue
B	LYS214
B	ASN216
B	ASN217
B	ASP218

---

site_id	AC8
Number of Residues	2
Details	binding site for residue SO4 B 402

Chain	Residue
B	LYS135
B	TRP333

---

site_id	AC9
Number of Residues	4
Details	binding site for residue SO4 B 403

Chain	Residue
B	THR219
B	HIS221
B	ALA234
C	LYS208

---

site_id	AD1
Number of Residues	2
Details	binding site for residue SO4 B 404

Chain	Residue
B	HIS215
B	ASN217

---

site_id	AD2
Number of Residues	8
Details	binding site for residue EQD B 405

Chain	Residue
B	ALA111
B	ASP149
B	ASN162
B	PHE195
B	THR245
B	ILE247
B	HOH503
B	HOH505

---

site_id	AD3
Number of Residues	1
Details	binding site for residue EDO B 406

Chain	Residue
B	EDO407

---

site_id	AD4
Number of Residues	5
Details	binding site for residue EDO B 407

Chain	Residue
B	HIS146
B	THR212
B	ARG237
B	EDO406
C	PRO236

---

site_id	AD5
Number of Residues	2
Details	binding site for residue EDO B 408

Chain	Residue
B	HOH507
C	EDO405

---

site_id	AD6
Number of Residues	2
Details	binding site for residue EDO B 409

Chain	Residue
B	LYS208
C	HIS221

---

site_id	AD7
Number of Residues	3
Details	binding site for residue EDO B 410

Chain	Residue
B	GLU224
B	GLU229
C	ARG156

---

site_id	AD8
Number of Residues	2
Details	binding site for residue EDO B 411

Chain	Residue
B	TRP282
B	HOH504

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
C	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":"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	1
Details	Modified residue: {"description":"Phosphothreonine; by CK2","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---