5ULS

Structure of GRP94 in the active conformation

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	19
Details	binding site for residue ANP A 801

Chain	Residue
A	ASN107
A	GLY193
A	GLN194
A	PHE195
A	GLY196
A	VAL197
A	GLY198
A	PHE199
A	THR245
A	ARG448
A	HOH917
A	ALA111
A	LYS114
A	MET154
A	ASN162
A	LYS168
A	SER169
A	GLY170
A	THR171

---

site_id	AC2
Number of Residues	19
Details	binding site for residue ANP B 801

Chain	Residue
B	GLU103
B	ASN107
B	ALA111
B	LYS114
B	MET154
B	ASN162
B	LYS168
B	SER169
B	GLY170
B	THR171
B	GLY193
B	GLN194
B	PHE195
B	GLY196
B	VAL197
B	GLY198
B	PHE199
B	THR245
B	ARG448

---

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	SITE: Important for ATP hydrolysis => ECO:0000269|PubMed:17936703

Chain	Residue	Details
A	ARG448
B	ARG448

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P14625

Chain	Residue	Details
A	SER64
A	SER447
B	SER64
B	SER447

---

site_id	SWS_FT_FI6
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_FI7
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q66HD0

Chain	Residue	Details
A	SER172
A	SER403
B	SER172
B	SER403

---

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P08113

Chain	Residue	Details
A	LYS404
A	LYS633
B	LYS404
B	LYS633

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P08113

Chain	Residue	Details
A	LYS479
B	LYS479

---

site_id	SWS_FT_FI10
Number of Residues	12
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255

Chain	Residue	Details
A	ASN62
B	ASN445
B	ASN481
B	ASN502
A	ASN107
A	ASN217
A	ASN445
A	ASN481
A	ASN502
B	ASN62
B	ASN107
B	ASN217

---