5WMT

Structure of GRP94 N-terminal Domain bound to resorcinylic inhibitor BnIm.

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue EDO A 401

Chain	Residue
A	HIS221
A	HOH504
C	LYS208

---

site_id	AC2
Number of Residues	2
Details	binding site for residue EDO A 402

Chain	Residue
A	LYS214
A	ASN216

---

site_id	AC3
Number of Residues	2
Details	binding site for residue EDO A 403

Chain	Residue
A	LYS135
A	TRP333

---

site_id	AC4
Number of Residues	2
Details	binding site for residue EDO A 404

Chain	Residue
A	LYS135
A	TYR280

---

site_id	AC5
Number of Residues	11
Details	binding site for residue 9QY A 405

Chain	Residue
A	ASN107
A	ALA111
A	ASP149
A	MET154
A	ASN162
A	PHE195
A	THR245
A	ILE247
A	HOH501
A	HOH503
A	HOH507

---

site_id	AC6
Number of Residues	7
Details	binding site for residue EDO B 401

Chain	Residue
B	SER169
B	LYS208
B	GLU224
B	ASP226
B	GLU229
B	PHE230
B	SER231

---

site_id	AC7
Number of Residues	3
Details	binding site for residue EDO B 402

Chain	Residue
B	ARG156
B	HIS221
D	LYS208

---

site_id	AC8
Number of Residues	2
Details	binding site for residue EDO B 403

Chain	Residue
B	THR212
B	ARG237

---

site_id	AC9
Number of Residues	2
Details	binding site for residue MG B 404

Chain	Residue
B	TRP282
B	TRP331

---

site_id	AD1
Number of Residues	10
Details	binding site for residue 9QY B 405

Chain	Residue
B	ASN107
B	ALA111
B	ASP149
B	MET154
B	ASN162
B	PHE195
B	TRP223
B	ILE247
B	HOH502
B	HOH504

---

site_id	AD2
Number of Residues	7
Details	binding site for residue EDO C 401

Chain	Residue
C	SER169
C	LYS208
C	GLU224
C	ASP226
C	GLU229
C	PHE230
C	SER231

---

site_id	AD3
Number of Residues	3
Details	binding site for residue EDO C 402

Chain	Residue
C	THR212
C	ARG237
C	EDO403

---

site_id	AD4
Number of Residues	1
Details	binding site for residue EDO C 403

Chain	Residue
C	EDO402

---

site_id	AD5
Number of Residues	3
Details	binding site for residue EDO C 404

Chain	Residue
A	LYS208
C	THR219
C	HIS221

---

site_id	AD6
Number of Residues	2
Details	binding site for residue MG C 405

Chain	Residue
C	TRP282
C	TRP331

---

site_id	AD7
Number of Residues	9
Details	binding site for residue 9QY C 406

Chain	Residue
C	ALA111
C	ASP149
C	MET154
C	ASN162
C	LEU163
C	PHE195
C	TRP223
C	ILE247
C	HOH503

---

site_id	AD8
Number of Residues	2
Details	binding site for residue EDO D 401

Chain	Residue
B	LYS208
D	HIS221

---

site_id	AD9
Number of Residues	2
Details	binding site for residue EDO D 402

Chain	Residue
D	LYS135
D	TRP333

---

site_id	AE1
Number of Residues	2
Details	binding site for residue EDO D 403

Chain	Residue
D	LYS214
D	ASN216

---

site_id	AE2
Number of Residues	5
Details	binding site for residue EDO D 404

Chain	Residue
B	VAL250
D	THR219
D	ALA234
D	ASP235
D	GLY238

---

site_id	AE3
Number of Residues	12
Details	binding site for residue 9QY D 405

Chain	Residue
D	ASN107
D	ALA111
D	ASP149
D	MET154
D	ASN162
D	LEU163
D	PHE195
D	THR245
D	ILE247
D	HOH502
D	HOH505
D	HOH507

---

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	4
Details	BINDING: BINDING => ECO:0000269|PubMed:15292259, ECO:0000269|PubMed:15951571, ECO:0000269|PubMed:17936703, ECO:0007744|PDB:1TC0, ECO:0007744|PDB:1TC6, ECO:0007744|PDB:1YT0, ECO:0007744|PDB:2O1U, ECO:0007744|PDB:2O1V

Chain	Residue	Details
C	ASN107
D	ASN107
A	ASN107
B	ASN107

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:15292259, ECO:0000269|PubMed:15951571, ECO:0000269|PubMed:17936703, ECO:0007744|PDB:1TBW, ECO:0007744|PDB:1TC0, ECO:0007744|PDB:1TC6, ECO:0007744|PDB:1YT0, ECO:0007744|PDB:2O1U, ECO:0007744|PDB:2O1V

Chain	Residue	Details
C	ASP149
C	PHE199
D	ASP149
D	PHE199
A	PHE199
B	ASP149
B	PHE199
A	ASP149

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:15292259, ECO:0000269|PubMed:15951571, ECO:0000269|PubMed:17936703, ECO:0007744|PDB:1TBW, ECO:0007744|PDB:1TC0, ECO:0007744|PDB:1TC6, ECO:0007744|PDB:2O1U, ECO:0007744|PDB:2O1V

Chain	Residue	Details
B	ASN162
C	ASN162
D	ASN162
A	ASN162

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P14625

Chain	Residue	Details
B	LYS168
C	LYS168
D	LYS168
A	LYS168

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q66HD0

Chain	Residue	Details
A	SER172
B	SER172
C	SER172
D	SER172

---

site_id	SWS_FT_FI6
Number of Residues	8
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
C	ASN107
C	ASN217
D	ASN107
D	ASN217
A	ASN107
A	ASN217
B	ASN107
B	ASN217

---