Structure of PDB 5eml Chain A

Receptor sequence
>5emlA (length=625) Species: 9606 (Homo sapiens) [Search protein sequence]
RVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNR
PGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELN
FGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPED
LRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADL
PSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRLLKLEV
QFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPL
QPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQVLM
VLGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQ
VTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGV
SIPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQL
SAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYQD
ITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVW
YEWAVTAPVCSAIHNPTGRSYTIGL
3D structure
PDB5eml Structure and Property Guided Design in the Identification of PRMT5 Tool Compound EPZ015666.
ChainA
Resolution2.39 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.1.1.320: type II 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 SAM A L315 Y324 Y334 G365 P370 E392 K393 D419 M420 E435 L436 C449 L303 Y312 Y322 G353 P358 E380 K381 D407 M408 E423 L424 C437
BS02 5QK A Y304 Q309 L312 L319 F327 E435 E444 V503 S578 W579 F580 Y292 Q297 L300 L307 F315 E423 E432 V491 S566 W567 F568 MOAD: ic50=23nM
PDBbind-CN: -logKd/Ki=7.64,IC50=23nM
BindingDB: IC50=<100nM
Gene Ontology
Molecular Function
GO:0002039 p53 binding
GO:0003714 transcription corepressor activity
GO:0005515 protein binding
GO:0008168 methyltransferase activity
GO:0008327 methyl-CpG binding
GO:0008469 histone arginine N-methyltransferase activity
GO:0016274 protein-arginine N-methyltransferase activity
GO:0035243 protein-arginine omega-N symmetric methyltransferase activity
GO:0042054 histone methyltransferase activity
GO:0042802 identical protein binding
GO:0043021 ribonucleoprotein complex binding
GO:0044020 histone H4R3 methyltransferase activity
GO:0044877 protein-containing complex binding
GO:0046982 protein heterodimerization activity
GO:0070888 E-box binding
GO:0140938 histone H3 methyltransferase activity
Biological Process
GO:0000387 spliceosomal snRNP assembly
GO:0006325 chromatin organization
GO:0006338 chromatin remodeling
GO:0006353 DNA-templated transcription termination
GO:0006355 regulation of DNA-templated transcription
GO:0006479 protein methylation
GO:0007088 regulation of mitotic nuclear division
GO:0010468 regulation of gene expression
GO:0018216 peptidyl-arginine methylation
GO:0032259 methylation
GO:0032922 circadian regulation of gene expression
GO:0035246 peptidyl-arginine N-methylation
GO:0042118 endothelial cell activation
GO:0044027 negative regulation of gene expression via chromosomal CpG island methylation
GO:0045596 negative regulation of cell differentiation
GO:0045892 negative regulation of DNA-templated transcription
GO:0048026 positive regulation of mRNA splicing, via spliceosome
GO:0048511 rhythmic process
GO:0048714 positive regulation of oligodendrocyte differentiation
GO:0070372 regulation of ERK1 and ERK2 cascade
GO:0090161 Golgi ribbon formation
GO:0097421 liver regeneration
GO:1901796 regulation of signal transduction by p53 class mediator
GO:1904992 positive regulation of adenylate cyclase-inhibiting dopamine receptor signaling pathway
Cellular Component
GO:0000785 chromatin
GO:0005634 nucleus
GO:0005654 nucleoplasm
GO:0005694 chromosome
GO:0005737 cytoplasm
GO:0005794 Golgi apparatus
GO:0005829 cytosol
GO:0032991 protein-containing complex
GO:0034709 methylosome
GO:0035097 histone methyltransferase complex

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:5eml, PDBe:5eml, PDBj:5eml
PDBsum5eml
PubMed26985292
UniProtO14744|ANM5_HUMAN Protein arginine N-methyltransferase 5 (Gene Name=PRMT5)

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