2GFD

GRP94 in complex with the novel HSP90 Inhibitor Radamide

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 RDA A 1001

Chain	Residue
A	ASN107
A	PHE199
A	TYR200
A	THR245
A	ILE247
A	HOH1004
A	HOH1005
A	HOH1007
A	HOH1084
A	ALA111
A	ASP149
A	MET154
A	ASN162
A	ILE166
A	LYS168
A	GLY196
A	VAL197

---

site_id	AC2
Number of Residues	18
Details	BINDING SITE FOR RESIDUE RDA B 1002

Chain	Residue
B	ASN107
B	ALA111
B	ASP149
B	MET154
B	ASN162
B	LEU163
B	ILE166
B	GLY196
B	VAL197
B	PHE199
B	TYR200
B	THR245
B	ILE247
B	HOH1003
B	HOH1006
B	HOH1043
B	HOH1093
B	HOH1140

---

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PG4 A 501

Chain	Residue
A	THR212
A	ARG237
A	THR248
A	PG4502
A	HOH1003
A	HOH1029
A	HOH1046
A	HOH1078
A	HOH1095
A	HOH1101
A	HOH1120

---

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PG4 A 502

Chain	Residue
A	LYS137
A	HIS146
A	THR148
A	PG4501
A	HOH1074

---

site_id	AC5
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PG4 B 504

Chain	Residue
B	THR212
B	ARG237
B	THR240
B	THR246
B	THR248
B	HOH1032
B	HOH1120
B	HOH1123

---

site_id	AC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE PG4 B 505

Chain	Residue
B	LYS137
B	THR148
B	TRP282

---

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 1PE B 601

Chain	Residue
A	ASN83
A	LYS87
A	ILE90
B	ASN83
B	LYS87
B	ILE90
B	SER227
B	HOH1069

---

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	GLY288
B	GLY288

---

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

---