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3LJ2

IRE1 complexed with JAK Inhibitor I

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
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE IZA A 1
ChainResidue
ALEU680
ALEU804
AASP828
ATYR682
AALA700
AGLU746
ALEU747
ACYS748
AASN749
ALEU750
AGLN801

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE IZA B 1
ChainResidue
BLEU680
BTYR682
BVAL689
BALA700
BGLU746
BLEU747
BCYS748
BASN749
BLEU750
BGLN801
BLEU804

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 Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP797
BASP797

site_idSWS_FT_FI2
Number of Residues14
DetailsBINDING: BINDING => ECO:0000269|PubMed:18191223, ECO:0007744|PDB:2RIO
ChainResidueDetails
ASER684
BGLU746
BCYS748
BASN751
BASN802
BASP828
ALYS702
AGLU746
ACYS748
AASN751
AASN802
AASP828
BSER684
BLYS702

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:18191223, ECO:0000305|PubMed:8670804
ChainResidueDetails
ASEP840
ASEP841
BSEP840
BSEP841

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:18191223
ChainResidueDetails
ATPO844
BTPO844

237735

PDB entries from 2025-06-18

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