Structure of PDB 1ori Chain A

Receptor sequence
>1oriA (length=316) Species: 10116 (Rattus norvegicus) [Search protein sequence]
SYAHFGIHEEMLKDEVRTLTYRNSMFHNRHLFKDKVVLDVGSGTGILCMF
AAKAGARKVIGIECSSISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEK
VDIIISEWMGYCLFYESMLNTVLHARDKWLAPDGLIFPDRATLYVTAIED
RQYKDYKIHWWENVYGFDMSCIKDVAIKEPLVDVVDPKQLVTNACLIKEV
DIYTVKVEDLTFTSPFCLQVKRNDYVHALVAYFNIEFTRCHKRTGFSTSP
ESPYTHWKQTVFYMEDYLTVKTGEEIFGTIGMRPNAKNNRDLDFTIDLDF
KGQLCELSCSTDYRMR
3D structure
PDB1ori Structure of the Predominant Protein Arginine Methyltransferase PRMT1 and Analysis of its Binding to Substrate Peptides
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D51 E144 E153 H293
Catalytic site (residue number reindexed from 1) D14 E107 E116 H256
Enzyme Commision number 2.1.1.319: type I protein arginine methyltransferase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 SAH A R54 G78 I83 E100 C101 V128 E144 M155 R17 G41 I46 E63 C64 V91 E107 M118
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:1ori, PDBe:1ori, PDBj:1ori
PDBsum1ori
PubMed12737817
UniProtQ63009|ANM1_RAT Protein arginine N-methyltransferase 1 (Gene Name=Prmt1)

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