Structure of PDB 3q7e Chain A Binding Site BS02

Receptor Information
>3q7e Chain A (length=313) Species: 10116 (Rattus norvegicus) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
HFGIHEELLKDEVRTLTYRNSMFHNRHLFKDKVVLDVGSGTGILCMFAAK
AGARKVIGIECSSISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEKVDI
IISEWMGYCLFYESMLNTVLHARDKWLAPDGLIFPDRATLYVTAIEDRQY
KDYKIHWWENVYGFDMSCIKDVAIKEPLVDVVDPKQLVTNACLIKEVDIY
TVKVEDLTFTSPFCLQVKRNDYVHALVAYFNIEFTRCHKRTGFSTSPESP
YTHWKQTVFYMEDYLTVKTGEEIFGTIGMRPNAKNNRDLDFTIDLDFKGQ
LCELSCSTDYRMR
Ligand information
Ligand IDMG
InChIInChI=1S/Mg/q+2
InChIKeyJLVVSXFLKOJNIY-UHFFFAOYSA-N
SMILES
SoftwareSMILES
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Mg+2]
CACTVS 3.341[Mg++]
FormulaMg
NameMAGNESIUM ION
ChEMBL
DrugBankDB01378
ZINC
PDB chain3q7e Chain A Residue 354 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB3q7e Investigation of the molecular origins of protein-arginine methyltransferase I (PRMT1) product specificity reveals a role for two conserved methionine residues.
Resolution2.2 Å
Binding residue
(original residue number in PDB)		R59 N60 F63
Binding residue
(residue number reindexed from 1)		R19 N20 F23
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) D51 E144 E153 H293
Catalytic site (residue number reindexed from 1) D11 E104 E113 H253
Enzyme Commision number 2.1.1.319: type I protein arginine methyltransferase.
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0008168 methyltransferase activity
GO:0008170 N-methyltransferase activity
GO:0008276 protein methyltransferase activity
GO:0008327 methyl-CpG binding
GO:0008757 S-adenosylmethionine-dependent methyltransferase activity
GO:0016274 protein-arginine N-methyltransferase activity
GO:0019899 enzyme binding
GO:0030519 snoRNP binding
GO:0035241 protein-arginine omega-N monomethyltransferase activity
GO:0035242 protein-arginine omega-N asymmetric methyltransferase activity
GO:0042054 histone methyltransferase activity
GO:0042802 identical protein binding
GO:0044020 histone H4R3 methyltransferase activity
GO:0048273 mitogen-activated protein kinase p38 binding
GO:0106080 GATOR1 complex binding
GO:1904047 S-adenosyl-L-methionine binding
Biological Process
GO:0001701 in utero embryonic development
GO:0006338 chromatin remodeling
GO:0006479 protein methylation
GO:0006974 DNA damage response
GO:0008284 positive regulation of cell population proliferation
GO:0008380 RNA splicing
GO:0018216 peptidyl-arginine methylation
GO:0019919 peptidyl-arginine methylation, to asymmetrical-dimethyl arginine
GO:0030510 regulation of BMP signaling pathway
GO:0031175 neuron projection development
GO:0032259 methylation
GO:0035247 peptidyl-arginine omega-N-methylation
GO:0045648 positive regulation of erythrocyte differentiation
GO:0045652 regulation of megakaryocyte differentiation
GO:0045653 negative regulation of megakaryocyte differentiation
GO:0045727 positive regulation of translation
GO:0046329 negative regulation of JNK cascade
GO:0046500 S-adenosylmethionine metabolic process
GO:0046985 positive regulation of hemoglobin biosynthetic process
GO:0048738 cardiac muscle tissue development
GO:0051260 protein homooligomerization
GO:0061431 cellular response to methionine
GO:0097421 liver regeneration
GO:1900745 positive regulation of p38MAPK cascade
GO:1904263 positive regulation of TORC1 signaling
GO:1905168 positive regulation of double-strand break repair via homologous recombination
Cellular Component
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005737 cytoplasm
GO:0005764 lysosome
GO:0005765 lysosomal membrane
GO:0005829 cytosol
GO:0016020 membrane
GO:0032991 protein-containing complex
GO:0034709 methylosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3q7e, PDBe:3q7e, PDBj:3q7e
PDBsum3q7e
PubMed21697082
UniProtQ63009|ANM1_RAT Protein arginine N-methyltransferase 1 (Gene Name=Prmt1)

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