Structure of PDB 7uyf Chain A

Receptor sequence
>7uyfA (length=623) Species: 9606 (Homo sapiens) [Search protein sequence]
RVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNR
PGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELN
FGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPED
LRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADL
PSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRLLKLEV
QFIITGTNHHKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQP
LMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQVLMVL
GAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQVT
VVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSI
PGEYTSFLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSA
PQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYQDIT
LSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWYE
WAVTAPVCSAIHNPTGRSYTIGL
3D structure
PDB7uyf Fragment optimization and elaboration strategies - the discovery of two lead series of PRMT5/MTA inhibitors from five fragment hits.
ChainA
Resolution2.82 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 PUI A F327 E435 L437 E444 S578 W579 F313 E421 L423 E430 S564 W565
BS02 MTA A L315 Y324 F327 G365 E392 K393 D419 M420 E435 L436 C449 L301 Y310 F313 G351 E378 K379 D405 M406 E421 L422 C435
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:7uyf, PDBe:7uyf, PDBj:7uyf
PDBsum7uyf
PubMed36545438
UniProtO14744|ANM5_HUMAN Protein arginine N-methyltransferase 5 (Gene Name=PRMT5)

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