Structure of PDB 6v0n Chain A
Receptor sequence
>6v0nA (length=624) Species:
9606
(Homo sapiens) [
Search protein sequence
]
VSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNRP
GPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNF
GAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDL
RDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLP
SNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRLLKLEVQ
FIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQ
PLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQVLMV
LGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQV
TVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVS
IPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLS
APQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYQDI
TLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWY
EWAVTAPVCSAIHNPTGRSYTIGL
3D structure
PDB
6v0n
Molecular basis for substrate recruitment to the PRMT5 methylosome.
Chain
A
Resolution
2.11 Å
3D
structure
[
Spin on
]
[
Spin off
]
[
Reset orientation
]
[
High quality
]
[
Low quality
]
[
White background
]
[
Black background
]
[
Download
]
[
Download structure with residue number starting from 1
]
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
N239 K240 F243 K248 Q251 Q282 Y283 Y286
N226 K227 F230 K235 Q238 Q269 Y270 Y273
BS02
SFG
A
P314 L315 Y324 Y334 G365 P370 E392 K393 D419 M420 E435 L436 C449
P301 L302 Y311 Y321 G352 P357 E379 K380 D406 M407 E422 L423 C436
BindingDB: IC50=8600nM
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:6v0n
,
PDBe:6v0n
,
PDBj:6v0n
PDBsum
6v0n
PubMed
34358446
UniProt
O14744
|ANM5_HUMAN Protein arginine N-methyltransferase 5 (Gene Name=PRMT5)
[
Back to BioLiP
]