Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3SDM

Structure of oligomeric kinase/RNase Ire1 in complex with an oligonucleotide

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
C	0004521	molecular_function	RNA endonuclease activity
C	0004540	molecular_function	RNA nuclease activity
C	0004672	molecular_function	protein kinase activity
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0005524	molecular_function	ATP binding
C	0006397	biological_process	mRNA processing
C	0006468	biological_process	protein phosphorylation
C	0030968	biological_process	endoplasmic reticulum unfolded protein response
D	0004521	molecular_function	RNA endonuclease activity
D	0004540	molecular_function	RNA nuclease activity
D	0004672	molecular_function	protein kinase activity
D	0004674	molecular_function	protein serine/threonine kinase activity
D	0005524	molecular_function	ATP binding
D	0006397	biological_process	mRNA processing
D	0006468	biological_process	protein phosphorylation
D	0030968	biological_process	endoplasmic reticulum unfolded protein response
E	0004521	molecular_function	RNA endonuclease activity
E	0004540	molecular_function	RNA nuclease activity
E	0004672	molecular_function	protein kinase activity
E	0004674	molecular_function	protein serine/threonine kinase activity
E	0005524	molecular_function	ATP binding
E	0006397	biological_process	mRNA processing
E	0006468	biological_process	protein phosphorylation
E	0030968	biological_process	endoplasmic reticulum unfolded protein response
F	0004521	molecular_function	RNA endonuclease activity
F	0004540	molecular_function	RNA nuclease activity
F	0004672	molecular_function	protein kinase activity
F	0004674	molecular_function	protein serine/threonine kinase activity
F	0005524	molecular_function	ATP binding
F	0006397	biological_process	mRNA processing
F	0006468	biological_process	protein phosphorylation
F	0030968	biological_process	endoplasmic reticulum unfolded protein response
G	0004521	molecular_function	RNA endonuclease activity
G	0004540	molecular_function	RNA nuclease activity
G	0004672	molecular_function	protein kinase activity
G	0004674	molecular_function	protein serine/threonine kinase activity
G	0005524	molecular_function	ATP binding
G	0006397	biological_process	mRNA processing
G	0006468	biological_process	protein phosphorylation
G	0030968	biological_process	endoplasmic reticulum unfolded protein response

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	7
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU00159, ECO:0000255\|PROSITE-ProRule:PRU10027

Chain	Residue	Details
A	ASP797
B	ASP797
C	ASP797
D	ASP797
E	ASP797
F	ASP797
G	ASP797

site_id	SWS_FT_FI2
Number of Residues	7
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU00159

Chain	Residue	Details
A	LEU680
B	LEU680
C	LEU680
D	LEU680
E	LEU680
F	LEU680
G	LEU680

site_id	SWS_FT_FI3
Number of Residues	7
Details	BINDING:

Chain	Residue	Details
A	LYS702
B	LYS702
C	LYS702
D	LYS702
E	LYS702
F	LYS702
G	LYS702

site_id	SWS_FT_FI4
Number of Residues	14
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000305\|PubMed:8670804

Chain	Residue	Details
A	SEP840
E	SEP841
F	SEP840
F	SEP841
G	SEP840
G	SEP841
A	SEP841
B	SEP840
B	SEP841
C	SEP840
C	SEP841
D	SEP840
D	SEP841
E	SEP840

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)