Structure of PDB 3r0q Chain G

Receptor sequence
>3r0qG (length=353) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
DYAQYFCTYSFLYHQKDMLSDRVRMDAYFNAVFQNKHHFEGKTVLDVGTG
SGILAIWSAQAGARKVYAVEATKMADHARALVKANNLDHIVEVIEGSVED
ISLPEKVDVIISEWMGYFLLRESMFDSVISARDRWLKPTGVMYPSHARMW
LAPIKSNIADRKRNDFDGAMADWHNFSDEIKSYYGVDMGVLTKPFAEEQE
KYYIQTAMWNDLNPQQIIGTPTIVKEMDCLTASVSEIEEVRSNVTSVINM
EHTRLCGFGGWFDVQFSGRKEDPAQQEIELTTAPSEQHCTHWGQQVFIMS
NPINVEEGDNLNLGLLMSRSKENHRLMEIELNCEIKEASGNPKESFKKTY
FIE
3D structure
PDB3r0q Crystal structure of the plant epigenetic protein arginine methyltransferase 10.
ChainG
Resolution2.61 Å
3D
structure
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Enzymatic activity
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 SAH G F36 Y39 M48 R54 G78 T79 E100 A101 G126 S127 E129 E143 M154 S157 F6 Y9 M18 R24 G48 T49 E70 A71 G96 S97 E99 E113 M124 S127
Gene Ontology
Molecular Function
GO:0008168 methyltransferase activity
GO:0008469 histone arginine N-methyltransferase activity
GO:0016274 protein-arginine N-methyltransferase activity
GO:0035241 protein-arginine omega-N monomethyltransferase activity
GO:0035242 protein-arginine omega-N asymmetric methyltransferase activity
Biological Process
GO:0006338 chromatin remodeling
GO:0010228 vegetative to reproductive phase transition of meristem
GO:0018216 peptidyl-arginine methylation
GO:0019919 peptidyl-arginine methylation, to asymmetrical-dimethyl arginine
GO:0032259 methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:3r0q, PDBe:3r0q, PDBj:3r0q
PDBsum3r0q
PubMed21986201
UniProtQ9MAT5|ANM10_ARATH Protein arginine N-methyltransferase PRMT10 (Gene Name=PRMT10)

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