Structure of PDB 1or8 Chain A
Receptor sequence
>1or8A (length=313) Species:
10116
(Rattus norvegicus) [
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HFGIHEEMLKDEVRTLTYRNSMFHNRHLFKDKVVLDVGSGTGILCMFAAK
AGARKVIGIECSSISDYAVKIVKANKLDHVVTIIKGKVEEVELPVEKVDI
IISEWMGYCLFYESMLNTVLHARDKWLAPDGLIFPDRATLYVTAIEDRQY
KDYKIHWWENVYGFDMSCIKDVAIKEPLVDVVDPKQLVTNACLIKEVDIY
TVKVEDLTFTSPFCLQVKRNDYVHALVAYFNIEFTRCHKRTGFSTSPESP
YTHWKQTVFYMEDYLTVKTGEEIFGTIGMRPNAKNNRDLDFTIDLDFKGQ
LCELSCSTDYRMR
3D structure
PDB
1or8
Structure of the Predominant Protein Arginine Methyltransferase PRMT1 and Analysis of Its Binding to Substrate Peptides
Chain
A
Resolution
2.35 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)
D11 E104 E113 H253
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
peptide
A
E47 M48 K50 D51 E144 W145 M146 Y148 E153 M155 H161 K243 Y291 H293
E7 M8 K10 D11 E104 W105 M106 Y108 E113 M115 H121 K203 Y251 H253
BS02
peptide
A
M48 E144 W145 M146 Y148 E153 M155 H161 K243 H293
M8 E104 W105 M106 Y108 E113 M115 H121 K203 H253
BS03
peptide
A
E47 M48 K50 D51 E144 W145 M146 Y148 E153 M155 Y291 H293
E7 M8 K10 D11 E104 W105 M106 Y108 E113 M115 Y251 H253
BS04
peptide
A
K235 D238 V242 F249 T250 G318 R320 D330 F331 D349
K195 D198 V202 F209 T210 G278 R280 D290 F291 D309
BS05
SAH
A
H45 R54 G78 S79 G80 I83 L84 E100 C101 G126 K127 E144 M155
H5 R14 G38 S39 G40 I43 L44 E60 C61 G86 K87 E104 M115
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
View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB
RCSB:1or8
,
PDBe:1or8
,
PDBj:1or8
PDBsum
1or8
PubMed
12737817
UniProt
Q63009
|ANM1_RAT Protein arginine N-methyltransferase 1 (Gene Name=Prmt1)
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