1YT0

Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N(DELTA)41 APO CRYSTAL SOAKED WITH ADP

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG A 338

Chain	Residue
A	HOH4
A	HOH5
A	ASN107
A	ADP339

---

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP A 339

Chain	Residue
A	HOH43
A	HOH50
A	ASN107
A	ALA111
A	ASP149
A	MET154
A	ASN162
A	LEU163
A	GLY198
A	PHE199
A	THR245
A	MG338
A	HOH1
A	HOH2
A	HOH4
A	HOH9
A	HOH11

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE PG4 A 301

Chain	Residue
A	LEU117
A	LEU120
A	THR212
A	ARG237
A	THR246
A	PG4302

---

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PG4 A 302

Chain	Residue
A	LYS137
A	HIS146
A	THR148
A	THR246
A	TRP282
A	PG4301
A	PG4307

---

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE PG4 A 306

Chain	Residue
A	HOH28
A	ASN83
A	MET86
A	LYS87
A	SER227

---

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE PG4 A 307

Chain	Residue
A	ASN129
A	LYS135
A	LYS137
A	THR148
A	THR150
A	LEU241
A	PG4302

---

site_id	AC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE PG4 A 308

Chain	Residue
A	SER92

---

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PG4 A 309

Chain	Residue
A	THR240
A	GLY242

---

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	1
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

---

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

Chain	Residue	Details
A	ASP149
A	PHE199

---

site_id	SWS_FT_FI3
Number of Residues	1
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

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P14625

Chain	Residue	Details
A	LYS168

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q66HD0

Chain	Residue	Details
A	SER172

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphothreonine; by CK2 => ECO:0000255

Chain	Residue	Details
A	GLY325

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphoserine; by CK2 => ECO:0000250|UniProtKB:P14625, ECO:0000255

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN107
A	ASN217

---