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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7BO7

CRYSTAL STRUCTURE OF THE HUMAN PRMT5:MEP50 COMPLEX with JNJB44355437

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
AAA0000387biological_processspliceosomal snRNP assembly
AAA0000785cellular_componentchromatin
AAA0002039molecular_functionp53 binding
AAA0003714molecular_functiontranscription corepressor activity
AAA0005515molecular_functionprotein binding
AAA0005634cellular_componentnucleus
AAA0005654cellular_componentnucleoplasm
AAA0005694cellular_componentchromosome
AAA0005737cellular_componentcytoplasm
AAA0005794cellular_componentGolgi apparatus
AAA0005829cellular_componentcytosol
AAA0006325biological_processchromatin organization
AAA0006338biological_processchromatin remodeling
AAA0006351biological_processDNA-templated transcription
AAA0006353biological_processDNA-templated transcription termination
AAA0006355biological_processregulation of DNA-templated transcription
AAA0006479biological_processprotein methylation
AAA0007088biological_processregulation of mitotic nuclear division
AAA0008168molecular_functionmethyltransferase activity
AAA0008327molecular_functionmethyl-CpG binding
AAA0010468biological_processregulation of gene expression
AAA0016274molecular_functionprotein-arginine N-methyltransferase activity
AAA0016740molecular_functiontransferase activity
AAA0018216biological_processpeptidyl-arginine methylation
AAA0032259biological_processmethylation
AAA0032922biological_processcircadian regulation of gene expression
AAA0032991cellular_componentprotein-containing complex
AAA0034709cellular_componentmethylosome
AAA0035097cellular_componenthistone methyltransferase complex
AAA0035243molecular_functionprotein-arginine omega-N symmetric methyltransferase activity
AAA0035246biological_processpeptidyl-arginine N-methylation
AAA0042054molecular_functionhistone methyltransferase activity
AAA0042118biological_processendothelial cell activation
AAA0042802molecular_functionidentical protein binding
AAA0043021molecular_functionribonucleoprotein complex binding
AAA0044020molecular_functionhistone H4R3 methyltransferase activity
AAA0044027biological_processnegative regulation of gene expression via chromosomal CpG island methylation
AAA0044877molecular_functionprotein-containing complex binding
AAA0045596biological_processnegative regulation of cell differentiation
AAA0045892biological_processnegative regulation of DNA-templated transcription
AAA0046982molecular_functionprotein heterodimerization activity
AAA0048026biological_processpositive regulation of mRNA splicing, via spliceosome
AAA0048511biological_processrhythmic process
AAA0048714biological_processpositive regulation of oligodendrocyte differentiation
AAA0070372biological_processregulation of ERK1 and ERK2 cascade
AAA0070888molecular_functionE-box binding
AAA0090161biological_processGolgi ribbon formation
AAA0097421biological_processliver regeneration
AAA0140938molecular_functionhistone H3 methyltransferase activity
AAA1901796biological_processregulation of signal transduction by p53 class mediator
AAA1904992biological_processpositive regulation of adenylate cyclase-inhibiting dopamine receptor signaling pathway
AAA2000234biological_processpositive regulation of rRNA processing
BBB0000209biological_processprotein polyubiquitination
BBB0000387biological_processspliceosomal snRNP assembly
BBB0003713molecular_functiontranscription coactivator activity
BBB0005515molecular_functionprotein binding
BBB0005634cellular_componentnucleus
BBB0005654cellular_componentnucleoplasm
BBB0005737cellular_componentcytoplasm
BBB0005794cellular_componentGolgi apparatus
BBB0005829cellular_componentcytosol
BBB0006511biological_processubiquitin-dependent protein catabolic process
BBB0008327molecular_functionmethyl-CpG binding
BBB0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
BBB0034709cellular_componentmethylosome
BBB0045893biological_processpositive regulation of DNA-templated transcription
BBB0048026biological_processpositive regulation of mRNA splicing, via spliceosome
BBB1990234cellular_componenttransferase complex
BBB1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
BBB2000234biological_processpositive regulation of rRNA processing
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. AVSGskDiCIKVWDL
ChainResidueDetails
BBBALA140-LEU154
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues307
DetailsDomain: {"description":"SAM-dependent MTase PRMT-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01015","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues279
DetailsRegion: {"description":"TIM barrel","evidences":[{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues172
DetailsRegion: {"description":"Beta barrel","evidences":[{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues6
DetailsRegion: {"description":"Dimerization","evidences":[{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues7
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Critical for specifying symmetric addition of methyl groups","evidences":[{"source":"UniProtKB","id":"P46580","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues53
DetailsRepeat: {"description":"WD 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues38
DetailsRepeat: {"description":"WD 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues39
DetailsRepeat: {"description":"WD 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues40
DetailsRepeat: {"description":"WD 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues40
DetailsRepeat: {"description":"WD 6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

248335

PDB entries from 2026-01-28

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