Structure of PDB 4gqb Chain A
Receptor sequence
>4gqbA (length=625) Species:
9606
(Homo sapiens) [
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RVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNR
PGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELN
FGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPED
LRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADL
PSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRLLKLEV
QFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPL
QPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQVLM
VLGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQ
VTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGV
SIPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQL
SAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYQD
ITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVW
YEWAVTAPVCSAIHNPTGRSYTIGL
3D structure
PDB
4gqb
Crystal structure of the human PRMT5:MEP50 complex.
Chain
A
Resolution
2.06 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
peptide
A
F300 Y307 Q309 S310 P311 L312 F327 E435 L437 E444 V503 S578 W579 F580
F288 Y295 Q297 S298 P299 L300 F315 E423 L425 E432 V491 S566 W567 F568
BS02
0XU
A
P314 L315 Y324 F327 Y334 G365 P370 E392 K393 D419 M420 E435 L436
P302 L303 Y312 F315 Y322 G353 P358 E380 K381 D407 M408 E423 L424
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
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:4gqb
,
PDBe:4gqb
,
PDBj:4gqb
PDBsum
4gqb
PubMed
23071334
UniProt
O14744
|ANM5_HUMAN Protein arginine N-methyltransferase 5 (Gene Name=PRMT5)
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