Structure of PDB 4ryl Chain A

Receptor sequence
>4rylA (length=300) Species: 9606 (Homo sapiens) [Search protein sequence]
HYGIHEEMLKDKIRTESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAK
AGAKKVLGVDQSEILYQAMDIIRLNKLEDTITLIKGKIEEVHLPVEKVDV
IISEWMGYFLLFESMLDSVLYAKNKYLAKGGSVYPDICTISLVAVSDVNK
HADRIAFWDDVYGFKMSCMKKAVIPEAVVEVLDPKTLISEPCGIKHIDCH
TTSISDLEFSSDFTLKITRTSMCTAIAGYFDIYFEKNCHNRVVFSTGPQS
TKTHWKQTVFLLEKPFSVKAGEALKGKVTVHKSLTVTLTLNNSTQTYGLQ
3D structure
PDB4ryl A Potent, Selective and Cell-Active Allosteric Inhibitor of Protein Arginine Methyltransferase 3 (PRMT3).
ChainA
Resolution2.1 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) D253 E346 E355 H496
Catalytic site (residue number reindexed from 1) D11 E104 E113 H254
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 3ZG A K392 H393 R396 V420 E422 T466 A467 K150 H151 R154 V178 E180 T224 A225 MOAD: Kd=53nM
PDBbind-CN: -logKd/Ki=7.28,Kd=53nM
BindingDB: IC50=91nM,EC50=2000nM
Gene Ontology
Molecular Function
GO:0016274 protein-arginine N-methyltransferase activity
Biological Process
GO:0018216 peptidyl-arginine methylation

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Molecular Function
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Biological Process
External links
PDB RCSB:4ryl, PDBe:4ryl, PDBj:4ryl
PDBsum4ryl
PubMed25728001
UniProtO60678|ANM3_HUMAN Protein arginine N-methyltransferase 3 (Gene Name=PRMT3)

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