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3SDM

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0004521molecular_functionRNA endonuclease activity
A0004540molecular_functionRNA nuclease activity
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006397biological_processmRNA processing
A0006468biological_processprotein phosphorylation
A0030968biological_processendoplasmic reticulum unfolded protein response
B0004521molecular_functionRNA endonuclease activity
B0004540molecular_functionRNA nuclease activity
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005524molecular_functionATP binding
B0006397biological_processmRNA processing
B0006468biological_processprotein phosphorylation
B0030968biological_processendoplasmic reticulum unfolded protein response
C0004521molecular_functionRNA endonuclease activity
C0004540molecular_functionRNA nuclease activity
C0004672molecular_functionprotein kinase activity
C0004674molecular_functionprotein serine/threonine kinase activity
C0005524molecular_functionATP binding
C0006397biological_processmRNA processing
C0006468biological_processprotein phosphorylation
C0030968biological_processendoplasmic reticulum unfolded protein response
D0004521molecular_functionRNA endonuclease activity
D0004540molecular_functionRNA nuclease activity
D0004672molecular_functionprotein kinase activity
D0004674molecular_functionprotein serine/threonine kinase activity
D0005524molecular_functionATP binding
D0006397biological_processmRNA processing
D0006468biological_processprotein phosphorylation
D0030968biological_processendoplasmic reticulum unfolded protein response
E0004521molecular_functionRNA endonuclease activity
E0004540molecular_functionRNA nuclease activity
E0004672molecular_functionprotein kinase activity
E0004674molecular_functionprotein serine/threonine kinase activity
E0005524molecular_functionATP binding
E0006397biological_processmRNA processing
E0006468biological_processprotein phosphorylation
E0030968biological_processendoplasmic reticulum unfolded protein response
F0004521molecular_functionRNA endonuclease activity
F0004540molecular_functionRNA nuclease activity
F0004672molecular_functionprotein kinase activity
F0004674molecular_functionprotein serine/threonine kinase activity
F0005524molecular_functionATP binding
F0006397biological_processmRNA processing
F0006468biological_processprotein phosphorylation
F0030968biological_processendoplasmic reticulum unfolded protein response
G0004521molecular_functionRNA endonuclease activity
G0004540molecular_functionRNA nuclease activity
G0004672molecular_functionprotein kinase activity
G0004674molecular_functionprotein serine/threonine kinase activity
G0005524molecular_functionATP binding
G0006397biological_processmRNA processing
G0006468biological_processprotein phosphorylation
G0030968biological_processendoplasmic reticulum unfolded protein response
Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpqNILV
ChainResidueDetails
AILE793-VAL805

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues49
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18191223","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RIO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues14
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"18191223","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8670804","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues7
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"18191223","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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