2EXL

GRP94 N-terminal Domain bound to geldanamycin

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 GDM A 301

Chain	Residue
A	ASN107
A	VAL197
A	GLY198
A	PHE199
A	THR245
A	HOH504
A	HOH505
A	HOH558
A	HOH592
A	ALA108
A	ASP110
A	LYS114
A	ASP149
A	MET154
A	ASN162
A	LEU163
A	GLY196

---

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE GDM B 302

Chain	Residue
B	ASN107
B	ALA108
B	ASP110
B	ALA111
B	LYS114
B	ASP149
B	MET154
B	ASN162
B	LEU163
B	GLY196
B	VAL197
B	GLY198
B	PHE199
B	HOH512
B	HOH513
B	HOH526
B	HOH541

---

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PG4 A 501

Chain	Residue
A	THR212
A	ARG237
A	THR240
A	THR248
A	PG4502
A	HOH507
A	HOH518
A	HOH574
A	HOH575
B	LEU117

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PG4 A 502

Chain	Residue
A	LYS137
A	HIS146
A	THR148
A	TRP282
A	PG4501
A	HOH503
A	HOH601

---

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PG4 B 508

Chain	Residue
A	LEU117
A	HOH598
B	LYS142
B	THR212
B	ARG237
B	THR248
B	PG4406
B	HOH539
B	HOH570
B	HOH601

---

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PG4 B 406

Chain	Residue
B	LYS137
B	HIS146
B	TRP282
B	PG4508
B	HOH599

---

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE 1PE A 409

Chain	Residue
A	ASN83
A	LYS87
A	SER227
A	HOH602
B	ASN83
B	LYS87
B	ILE90
B	HOH523

---

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

---