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4PL3

Crystal structure of murine IRE1 in complex with MKC9989 inhibitor

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 Residues7
Detailsbinding site for residue 31J A 1001
ChainResidue
APHE889
ATYR892
AASN906
ALYS907
AHIS910
BARG864
BGLN946

site_idAC2
Number of Residues12
Detailsbinding site for residue ADP A 1002
ChainResidue
AGLY580
AVAL586
ALYS599
AILE642
AGLU643
ACYS645
AHIS692
AASN693
AASP711
AMG1003
ALEU577
AHIS579

site_idAC3
Number of Residues4
Detailsbinding site for residue MG A 1003
ChainResidue
AHIS692
AASN693
AASP711
AADP1002

site_idAC4
Number of Residues13
Detailsbinding site for residue ADP B 1002
ChainResidue
BLEU577
BHIS579
BGLY580
BVAL586
BLYS599
BGLU643
BCYS645
BLYS690
BHIS692
BASN693
BLEU695
BASP711
BMG1003

site_idAC5
Number of Residues4
Detailsbinding site for residue MG B 1003
ChainResidue
BHIS692
BASN693
BASP711
BADP1002

site_idAC6
Number of Residues15
Detailsbinding site for Di-peptide 31J B 1001 and LYS B 907
ChainResidue
AARG864
BLEU882
BASP885
BLEU886
BPHE889
BTYR892
BALA903
BMET904
BASN906
BLYS908
BHIS909
BHIS910
BTYR911
BGLU913
BLEU914

Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKphNILL
ChainResidueDetails
AILE684-LEU696

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor; for protein kinase activity => 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:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:25164867, ECO:0007744|PDB:4PL5
ChainResidueDetails
ALEU577
BLEU577

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:25164867, ECO:0007744|PDB:4PL3, ECO:0007744|PDB:4PL4, ECO:0007744|PDB:4PL5
ChainResidueDetails
ALYS599
BLYS599

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:25164867, ECO:0007744|PDB:4PL3, ECO:0007744|PDB:4PL4, ECO:0007744|PDB:4PL5
ChainResidueDetails
AGLU643
ALYS690
AASP711
BGLU643
BLYS690
BASP711

site_idSWS_FT_FI5
Number of Residues2
DetailsSITE: Interacts with hydroxy-aryl-aldehyde inhibitors => ECO:0000269|PubMed:25164867
ChainResidueDetails
ATYR892
BTYR892

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:O75460
ChainResidueDetails
ASER724
BSER724

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000269|PubMed:35975910
ChainResidueDetails
ASER729
BSER729

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PDB entries from 2024-10-30

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