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6URC

Crystal structure of IRE1a in complex with compound 18

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 Residues17
Detailsbinding site for residue QFV A 1001
ChainResidue
ALEU577
ACYS645
AALA646
AGLU651
ASER710
AASP711
APHE712
AHOH1174
AHOH1253
AALA597
ALYS599
AGLU612
ALEU616
AILE640
AILE642
AGLU643
ALEU644

site_idAC2
Number of Residues7
Detailsbinding site for residue GOL A 1002
ChainResidue
AASP592
AARG594
APHE629
BGLU621
BARG627
BTYR628
BPHE629

site_idAC3
Number of Residues15
Detailsbinding site for residue QFV B 1001
ChainResidue
BLEU577
BALA597
BLYS599
BGLU612
BILE640
BILE642
BGLU643
BLEU644
BCYS645
BGLU651
BSER710
BASP711
BPHE712
BHOH1182
BHOH1226

Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKphNILI
ChainResidueDetails
AILE684-ILE696

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P32361, ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP688
BASP688

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P32361, ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU577
BLEU577

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:21317875, ECO:0000269|PubMed:9637683, ECO:0007744|PDB:3P23
ChainResidueDetails
ALYS599
BLYS599

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:21317875, ECO:0007744|PDB:3P23
ChainResidueDetails
AGLU643
ALYS690
AASP711
BGLU643
BLYS690
BASP711

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Interacts with hydroxy-aryl-aldehyde inhibitors => ECO:0000250|UniProtKB:Q9EQY0
ChainResidueDetails
ATYR892
BTYR892

site_idSWS_FT_FI6
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:30118681
ChainResidueDetails
ASER724
ASER729
BSER724
BSER729

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ATHR973
BTHR973

220113

PDB entries from 2024-05-22

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