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8X8Q

Structure of enterovirus protease in complex host factor

Functional Information from GO Data
ChainGOidnamespacecontents
B0000785cellular_componentchromatin
B0003713molecular_functiontranscription coactivator activity
B0003779molecular_functionactin binding
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0006338biological_processchromatin remodeling
B0008168molecular_functionmethyltransferase activity
B0016279molecular_functionprotein-lysine N-methyltransferase activity
B0016740molecular_functiontransferase activity
B0018021biological_processpeptidyl-histidine methylation
B0018023biological_processpeptidyl-lysine trimethylation
B0018064molecular_functionprotein-L-histidine N-tele-methyltransferase activity
B0030047biological_processactin modification
B0032259biological_processmethylation
B0042800molecular_functionhistone H3K4 methyltransferase activity
B0045893biological_processpositive regulation of DNA-templated transcription
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0046975molecular_functionhistone H3K36 methyltransferase activity
B0061629molecular_functionRNA polymerase II-specific DNA-binding transcription factor binding
B0070472biological_processregulation of uterine smooth muscle contraction
F0000166molecular_functionnucleotide binding
F0001172biological_processRNA-templated transcription
F0003723molecular_functionRNA binding
F0003968molecular_functionRNA-directed RNA polymerase activity
F0004386molecular_functionhelicase activity
F0005524molecular_functionATP binding
F0006508biological_processproteolysis
F0006811biological_processmonoatomic ion transport
F0008233molecular_functionpeptidase activity
F0008234molecular_functioncysteine-type peptidase activity
F0008270molecular_functionzinc ion binding
F0015267molecular_functionchannel activity
F0016032biological_processviral process
F0016740molecular_functiontransferase activity
F0016779molecular_functionnucleotidyltransferase activity
F0016787molecular_functionhydrolase activity
F0017111molecular_functionribonucleoside triphosphate phosphatase activity
F0019028cellular_componentviral capsid
F0019062biological_processvirion attachment to host cell
F0033644cellular_componenthost cell membrane
F0034220biological_processmonoatomic ion transmembrane transport
F0039520biological_processsymbiont-mediated activation of host autophagy
F0039522biological_processsymbiont-mediated suppression of host mRNA export from nucleus
F0039618cellular_componentT=pseudo3 icosahedral viral capsid
F0039657biological_processsymbiont-mediated suppression of host gene expression
F0042025cellular_componenthost cell nucleus
F0044162cellular_componenthost cell cytoplasmic vesicle membrane
F0044423cellular_componentvirion component
F0044694biological_processsymbiont genome entry into host cell via pore formation in plasma membrane
F0046718biological_processsymbiont entry into host cell
F0046872molecular_functionmetal ion binding
F0052031biological_processsymbiont-mediated perturbation of host defense response
F0052170biological_processsymbiont-mediated suppression of host innate immune response
F0075509biological_processendocytosis involved in viral entry into host cell
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues220
DetailsDomain: {"description":"SET","evidences":[{"source":"PROSITE-ProRule","id":"PRU00190","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30626964","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30785395","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31388018","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31911441","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31993215","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"32503840","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUN-2011","submissionDatabase":"PDB data bank","title":"Crystal structure of human SET domain-containing protein 3.","authors":["Zeng H.","Dong A.","Walker J.R.","Loppnau P.","Bountra C.","Weigelt J.","Arrowsmith C.H.","Edwards A.M.","Min J.","Wu H."]}},{"source":"PDB","id":"3SMT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6ICT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6ICV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6JAT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6MBJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6MBK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6MBL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OX0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OX1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OX2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OX3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OX4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6OX5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6V62","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6V63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WK1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6WK2","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

249524

PDB entries from 2026-02-18

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