Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

7ZUY

HUMAN PRMT5:MEP50 Crystal Structure With MTA and Fragment Bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0000387biological_processspliceosomal snRNP assembly
A0000785cellular_componentchromatin
A0002039molecular_functionp53 binding
A0003714molecular_functiontranscription corepressor activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005694cellular_componentchromosome
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0006325biological_processchromatin organization
A0006338biological_processchromatin remodeling
A0006353biological_processDNA-templated transcription termination
A0006355biological_processregulation of DNA-templated transcription
A0006479biological_processprotein methylation
A0007088biological_processregulation of mitotic nuclear division
A0008168molecular_functionmethyltransferase activity
A0008327molecular_functionmethyl-CpG binding
A0010468biological_processregulation of gene expression
A0016274molecular_functionprotein-arginine N-methyltransferase activity
A0016740molecular_functiontransferase activity
A0018216biological_processpeptidyl-arginine methylation
A0032259biological_processmethylation
A0032922biological_processcircadian regulation of gene expression
A0032991cellular_componentprotein-containing complex
A0034709cellular_componentmethylosome
A0035097cellular_componenthistone methyltransferase complex
A0035243molecular_functionprotein-arginine omega-N symmetric methyltransferase activity
A0035246biological_processpeptidyl-arginine N-methylation
A0042054molecular_functionhistone methyltransferase activity
A0042118biological_processendothelial cell activation
A0042802molecular_functionidentical protein binding
A0043021molecular_functionribonucleoprotein complex binding
A0044020molecular_functionhistone H4R3 methyltransferase activity
A0044027biological_processnegative regulation of gene expression via chromosomal CpG island methylation
A0044877molecular_functionprotein-containing complex binding
A0045596biological_processnegative regulation of cell differentiation
A0045892biological_processnegative regulation of DNA-templated transcription
A0046982molecular_functionprotein heterodimerization activity
A0048026biological_processpositive regulation of mRNA splicing, via spliceosome
A0048511biological_processrhythmic process
A0048714biological_processpositive regulation of oligodendrocyte differentiation
A0070372biological_processregulation of ERK1 and ERK2 cascade
A0070888molecular_functionE-box binding
A0090161biological_processGolgi ribbon formation
A0097421biological_processliver regeneration
A0140938molecular_functionhistone H3 methyltransferase activity
A1901796biological_processregulation of signal transduction by p53 class mediator
A1904992biological_processpositive regulation of adenylate cyclase-inhibiting dopamine receptor signaling pathway
B0000209biological_processprotein polyubiquitination
B0000387biological_processspliceosomal snRNP assembly
B0003713molecular_functiontranscription coactivator activity
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0006357biological_processregulation of transcription by RNA polymerase II
B0006511biological_processubiquitin-dependent protein catabolic process
B0007309biological_processoocyte axis specification
B0008284biological_processpositive regulation of cell population proliferation
B0008285biological_processnegative regulation of cell population proliferation
B0008327molecular_functionmethyl-CpG binding
B0031465cellular_componentCul4B-RING E3 ubiquitin ligase complex
B0034709cellular_componentmethylosome
B0045893biological_processpositive regulation of DNA-templated transcription
B0048026biological_processpositive regulation of mRNA splicing, via spliceosome
B0060528biological_processsecretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development
B0060767biological_processepithelial cell proliferation involved in prostate gland development
B0060770biological_processnegative regulation of epithelial cell proliferation involved in prostate gland development
B1990234cellular_componenttransferase complex
B1990756molecular_functionubiquitin-like ligase-substrate adaptor activity
Functional Information from PROSITE/UniProt
site_idPS00678
Number of Residues15
DetailsWD_REPEATS_1 Trp-Asp (WD) repeats signature. AVSGskDiCIKVWDL
ChainResidueDetails
BALA140-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 Residues41
DetailsRepeat: {"description":"WD 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues40
DetailsRepeat: {"description":"WD 6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

PDB statisticsPDBj update infoContact PDBjnumon