5TTZ

Crystal structure of Grp94 bound to isoform-selective inhibitor methyl 2-(2-(1-(4-bromobenzyl)-1H-imidazol-2-yl)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	9
Details	binding site for residue 7KY A 401

Chain	Residue
A	ASN107
A	ALA111
A	ASP149
A	MET154
A	ASN162
A	GLY196
A	PHE199
A	ILE247
A	HOH504

---

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

Chain	Residue
A	THR212
A	ARG237
A	HOH501

---

site_id	AC3
Number of Residues	13
Details	binding site for residue 7KY B 401

Chain	Residue
B	ASN107
B	ALA111
B	LYS114
B	ASP149
B	VAL152
B	MET154
B	ASN162
B	GLY196
B	PHE199
B	THR245
B	ILE247
B	HOH504
B	HOH507

---

site_id	AC4
Number of Residues	4
Details	binding site for residue PG4 B 402

Chain	Residue
B	LYS137
B	THR246
B	PGE403
B	HOH505

---

site_id	AC5
Number of Residues	6
Details	binding site for residue PGE B 403

Chain	Residue
B	THR212
B	ARG237
B	THR240
B	THR248
B	PG4402
B	HOH501

---

site_id	AC6
Number of Residues	4
Details	binding site for residue PE4 B 404

Chain	Residue
B	ASN83
B	LYS87
B	ILE90
B	SER227

---

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	2
Details	MOD_RES: Phosphothreonine; by CK2 => ECO:0000255

Chain	Residue	Details
A	GLY325
B	GLY325

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P14625, ECO:0000255

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN107
A	ASN217
B	ASN107
B	ASN217

---