3O2F

Structure of the N-domain of GRP94 bound to the HSP90 inhibitor PU-H54

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	13
Details	BINDING SITE FOR RESIDUE P54 A 1

Chain	Residue
A	HOH17
A	PHE199
A	ALA202
A	ILE247
A	HOH441
A	HOH22
A	HOH40
A	ASN107
A	ASP110
A	ALA111
A	ASP149
A	MET154
A	PHE195

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE IPA A 338

Chain	Residue
A	LYS135
A	TYR280

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA A 2

Chain	Residue
A	MET86
A	ILE89
A	HOH401
B	TYR94

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL A 3

Chain	Residue
A	ARG237
A	GLY238
A	ASN239
A	HOH396

---

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

Chain	Residue
A	GLU224
A	ASP226
A	GLU229
A	PHE230

---

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE IPA A 5

Chain	Residue
A	SER92
A	ASN96
B	LEU93
B	ARG102

---

site_id	AC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE P54 B 1

Chain	Residue
B	ASN107
B	ALA111
B	LYS114
B	ASP149
B	MET154
B	LEU163
B	PHE195
B	GLY198
B	PHE199
B	ALA202
B	HOH365
B	HOH391

---

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: 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
A	ASN107
B	ASN107

---

site_id	SWS_FT_FI2
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:1YT0, ECO:0007744|PDB:2O1U, ECO:0007744|PDB:2O1V

Chain	Residue	Details
A	ASP149
A	PHE199
B	ASP149
B	PHE199

---

site_id	SWS_FT_FI3
Number of Residues	2
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
A	ASN162
B	ASN162

---

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

Chain	Residue	Details
A	LYS168
B	LYS168

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q66HD0

Chain	Residue	Details
A	SER172
B	SER172

---

site_id	SWS_FT_FI6
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN107
A	ASN217
B	ASN107
B	ASN217

---