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1F3L

CRYSTAL STRUCTURE OF THE CONSERVED CORE OF PROTEIN ARGININE METHYLTRANSFERASE PRMT3

Functional Information from GO Data
ChainGOidnamespacecontents
A0016274molecular_functionprotein-arginine N-methyltransferase activity
A0018216biological_processpeptidyl-arginine methylation
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE SAH A 529
ChainResidue
AHOH4
ACYS261
AILE265
AASP282
AGLN283
ASER284
AGLY308
ALYS309
AILE310
AGLU311
AGLU326
AHOH42
AMET337
ASER340
AHOH43
AHOH51
APHE218
ATYR221
AMET230
AARG236
AGLY260

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues314
DetailsDomain: {"description":"SAM-dependent MTase PRMT-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01015","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"10899106","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10899106","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1F3L","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1or8
ChainResidueDetails
AGLU326
AGLU335

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PDB entries from 2025-12-10

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