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3LJ0

IRE1 complexed with ADP and Quercetin

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 Residues3
DetailsBINDING SITE FOR RESIDUE MG A 2102
ChainResidue
AASN802
AASP828
AADP2101

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SR A 2103
ChainResidue
AASP828
AADP2101

site_idAC3
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ADP A 2101
ChainResidue
AVAL689
AALA700
ALYS702
AGLU746
ACYS748
AASN751
AGLN801
AASN802
ALEU804
AASP828
AMG2102
ASR2103
AGLY681
ATYR682
AGLY683
ASER684

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 2102
ChainResidue
BASN802
BASP828
BADP2101

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE SR B 2103
ChainResidue
BASP828
BADP2101

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ADP B 2101
ChainResidue
BGLY681
BTYR682
BGLY683
BSER684
BTHR687
BVAL689
BALA700
BLYS702
BGLU746
BCYS748
BASN751
BGLN801
BASN802
BLEU804
BASP828
BMG2102
BSR2103

site_idAC7
Number of Residues9
DetailsBINDING SITE FOR RESIDUE QUE A 1
ChainResidue
APRO982
ASER984
ALYS985
ALYS992
AGLU1111
APHE1112
BQUE1
BGLU988
BPRO1077

site_idAC8
Number of Residues9
DetailsBINDING SITE FOR RESIDUE QUE B 1
ChainResidue
AQUE1
AGLU988
APRO1077
BPRO982
BSER984
BLYS985
BLYS992
BGLU1111
BPHE1112

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 Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU680
BLEU680

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS702
BLYS702

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000305|PubMed:8670804
ChainResidueDetails
ASEP840
ASEP841
BSEP840
BSEP841

221051

PDB entries from 2024-06-12

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