Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1ORI

Structure of the predominant protein arginine methyltransferase PRMT1

Functional Information from GO Data
ChainGOidnamespacecontents
A0001701biological_processin utero embryonic development
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005764cellular_componentlysosome
A0005765cellular_componentlysosomal membrane
A0005829cellular_componentcytosol
A0006338biological_processchromatin remodeling
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
A0016020cellular_componentmembrane
A0016274molecular_functionprotein-arginine N-methyltransferase activity
A0018216biological_processpeptidyl-arginine methylation
A0019899molecular_functionenzyme binding
A0019919biological_processpeptidyl-arginine methylation, to asymmetrical-dimethyl arginine
A0030510biological_processregulation of BMP signaling pathway
A0030519molecular_functionsnoRNP binding
A0031175biological_processneuron projection development
A0032259biological_processmethylation
A0032991cellular_componentprotein-containing complex
A0034709cellular_componentmethylosome
A0035241molecular_functionprotein-arginine omega-N monomethyltransferase activity
A0035242molecular_functionprotein-arginine omega-N asymmetric methyltransferase activity
A0035247biological_processpeptidyl-arginine omega-N-methylation
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
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
A0097421biological_processliver regeneration
A0106080molecular_functionGATOR1 complex binding
A1900745biological_processpositive regulation of p38MAPK cascade
A1904047molecular_functionS-adenosyl-L-methionine binding
A1904263biological_processpositive regulation of TORC1 signaling
A1905168biological_processpositive 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 354
ChainResidue
AHIS45
AGLY126
ALYS127
AVAL128
AGLU144
AMET155
AHOH372
AHOH373
AHOH374
AUNL700
AMET48
AARG54
AGLY78
AGLY80
AILE83
AGLU100
ACYS101
ASER102

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE UNL A 355
ChainResidue
AARG177
ATHR179
ATYR181
AASN271
AGLU273

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE UNL A 700
ChainResidue
AMET48
AGLU144
AMET146
ASAH354

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:12737817
ChainResidueDetails
AGLU144
AGLU153

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:12737817
ChainResidueDetails
AHIS45
AARG54
AGLY78
AGLU100
AGLU129

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9JIF0
ChainResidueDetails
ALYS116

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9JIF0
ChainResidueDetails
ALYS210
ALYS215

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q99873
ChainResidueDetails
ASER286
ASER289

site_idSWS_FT_FI6
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q9JIF0
ChainResidueDetails
ALYS127

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1or8
ChainResidueDetails
AGLU144
AGLU153

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

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon