3LJ0

IRE1 complexed with ADP and Quercetin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004521	molecular_function	RNA endonuclease activity
A	0004540	molecular_function	RNA nuclease activity
A	0004672	molecular_function	protein kinase activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005524	molecular_function	ATP binding
A	0006397	biological_process	mRNA processing
A	0006468	biological_process	protein phosphorylation
A	0030968	biological_process	endoplasmic reticulum unfolded protein response
B	0004521	molecular_function	RNA endonuclease activity
B	0004540	molecular_function	RNA nuclease activity
B	0004672	molecular_function	protein kinase activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0005524	molecular_function	ATP binding
B	0006397	biological_process	mRNA processing
B	0006468	biological_process	protein phosphorylation
B	0030968	biological_process	endoplasmic reticulum unfolded protein response

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 2102

Chain	Residue
A	ASN802
A	ASP828
A	ADP2101

---

site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SR A 2103

Chain	Residue
A	ASP828
A	ADP2101

---

site_id	AC3
Number of Residues	16
Details	BINDING SITE FOR RESIDUE ADP A 2101

Chain	Residue
A	VAL689
A	ALA700
A	LYS702
A	GLU746
A	CYS748
A	ASN751
A	GLN801
A	ASN802
A	LEU804
A	ASP828
A	MG2102
A	SR2103
A	GLY681
A	TYR682
A	GLY683
A	SER684

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG B 2102

Chain	Residue
B	ASN802
B	ASP828
B	ADP2101

---

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SR B 2103

Chain	Residue
B	ASP828
B	ADP2101

---

site_id	AC6
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ADP B 2101

Chain	Residue
B	GLY681
B	TYR682
B	GLY683
B	SER684
B	THR687
B	VAL689
B	ALA700
B	LYS702
B	GLU746
B	CYS748
B	ASN751
B	GLN801
B	ASN802
B	LEU804
B	ASP828
B	MG2102
B	SR2103

---

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE QUE A 1

Chain	Residue
A	PRO982
A	SER984
A	LYS985
A	LYS992
A	GLU1111
A	PHE1112
B	QUE1
B	GLU988
B	PRO1077

---

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE QUE B 1

Chain	Residue
A	QUE1
A	GLU988
A	PRO1077
B	PRO982
B	SER984
B	LYS985
B	LYS992
B	GLU1111
B	PHE1112

---

Functional Information from PROSITE/UniProt

site_id	PS00108
Number of Residues	13
Details	PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpqNILV

Chain	Residue	Details
A	ILE793-VAL805

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18191223","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RIO","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"18191223","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8670804","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"18191223","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---