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3Q7E

Crystal Structure of rat Protein Arginine Methyltransferase 1 (PRMT1)M48L mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0000724biological_processdouble-strand break repair via homologous recombination
A0001701biological_processin utero embryonic development
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005765cellular_componentlysosomal membrane
A0005829cellular_componentcytosol
A0006338biological_processchromatin remodeling
A0006355biological_processregulation of DNA-templated transcription
A0006479biological_processprotein methylation
A0006974biological_processDNA damage response
A0008168molecular_functionmethyltransferase activity
A0008170molecular_functionN-methyltransferase activity
A0008276molecular_functionprotein methyltransferase activity
A0008284biological_processpositive regulation of cell population proliferation
A0008327molecular_functionmethyl-CpG binding
A0008380biological_processRNA splicing
A0008757molecular_functionS-adenosylmethionine-dependent methyltransferase activity
A0016274molecular_functionprotein-arginine N-methyltransferase activity
A0016740molecular_functiontransferase activity
A0017148biological_processnegative regulation of translation
A0018216biological_processpeptidyl-arginine methylation
A0019899molecular_functionenzyme binding
A0019919biological_processpeptidyl-arginine methylation, to asymmetrical-dimethyl arginine
A0030509biological_processBMP signaling pathway
A0030510biological_processregulation of BMP signaling pathway
A0030514biological_processnegative regulation of BMP signaling pathway
A0030519molecular_functionsnoRNP binding
A0031175biological_processneuron projection development
A0031669biological_processcellular response to nutrient levels
A0032259biological_processmethylation
A0032991cellular_componentprotein-containing complex
A0034198biological_processcellular response to amino acid starvation
A0034709cellular_componentmethylosome
A0035241molecular_functionprotein-arginine omega-N monomethyltransferase activity
A0035242molecular_functionprotein-arginine omega-N asymmetric methyltransferase activity
A0035247biological_processpeptidyl-arginine omega-N-methylation
A0038202biological_processTORC1 signaling
A0042054molecular_functionhistone methyltransferase activity
A0042802molecular_functionidentical protein binding
A0044020molecular_functionhistone H4R3 methyltransferase activity
A0045648biological_processpositive regulation of erythrocyte differentiation
A0045652biological_processregulation of megakaryocyte differentiation
A0045653biological_processnegative regulation of megakaryocyte differentiation
A0045727biological_processpositive regulation of translation
A0045947biological_processnegative regulation of translational initiation
A0046329biological_processnegative regulation of JNK cascade
A0046500biological_processS-adenosylmethionine metabolic process
A0046985biological_processpositive regulation of hemoglobin biosynthetic process
A0048273molecular_functionmitogen-activated protein kinase p38 binding
A0048738biological_processcardiac muscle tissue development
A0051260biological_processprotein homooligomerization
A0061431biological_processcellular response to methionine
A0061462biological_processprotein localization to lysosome
A0097421biological_processliver regeneration
A0106080molecular_functionGATOR1 complex binding
A0140694biological_processmembraneless organelle assembly
A1900745biological_processpositive regulation of p38MAPK cascade
A1904047molecular_functionS-adenosyl-L-methionine binding
A1904262biological_processnegative regulation of TORC1 signaling
A1904263biological_processpositive regulation of TORC1 signaling
A1905168biological_processpositive regulation of double-strand break repair via homologous recombination
A2000042biological_processnegative regulation of double-strand break repair via homologous recombination
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE SAH A 1
ChainResidue
AHIS45
AGLY126
ALYS127
AVAL128
AGLU129
AGLU144
AMET155
AHOH355
AHOH363
AHOH364
ALEU48
AARG54
AGLY78
ASER79
AILE83
ALEU84
AGLU100
ACYS101

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 354
ChainResidue
AARG59
AASN60
APHE63

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"12737817","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12737817","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"Q9JIF0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9JIF0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q99873","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"Q9JIF0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues4
DetailsM-CSA 872
ChainResidueDetails
AASP51proton shuttle (general acid/base)
AGLU144electrostatic stabiliser
AGLU153electrostatic stabiliser
AHIS293proton shuttle (general acid/base)

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PDB entries from 2025-10-22

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