Reaction Details Report a problem with these data
Target
Protein arginine N-methyltransferase 3
Ligand
BDBM178103
Substrate
n/a
Meas. Tech.
ChEMBL_2146489 (CHEMBL5030835)
IC50
4.0±n/a nM
Citation
Shen, Y; Li, F; Szewczyk, MM; Halabelian, L; Chau, I; Eram, MS; Dela Seña, C; Park, KS; Meng, F; Chen, H; Zeng, H; Dong, A; Wu, H; Trush, VV; McLeod, D; Zepeda-Velázquez, CA; Campbell, RM; Mader, MM; Watson, BM; Schapira, M; Arrowsmith, CH; Al-Awar, R; Barsyte-Lovejoy, D; Kaniskan, HÜ; Brown, PJ; Vedadi, M; Jin, J A First-in-Class, Highly Selective and Cell-Active Allosteric Inhibitor of Protein Arginine Methyltransferase 6. J Med Chem 64:3697-3706 (2021) [PubMed] Article
More Info.:
Target
Name:
Protein arginine N-methyltransferase 3
Synonyms:
2.1.1.- | ANM3_HUMAN | HRMT1L3 | Heterogeneous nuclear ribonucleoprotein methyltransferase-like protein 3 | PRMT3 | Protein arginine N-methyltransferase 3
Type:
PROTEIN
Mol. Mass.:
59886.87
Organism:
Homo sapiens
Description:
ChEMBL_101368
Residue:
531
Sequence:
MCSLASGATGGRGAVENEEDLPELSDSGDEAAWEDEDDADLPHGKQQTPCLFCNRLFTSAEETFSHCKSEHQFNIDSMVHKHGLEFYGYIKLINFIRLKNPTVEYMNSIYNPVPWEKEEYLKPVLEDDLLLQFDVEDLYEPVSVPFSYPNGLSENTSVVEKLKHMEARALSAEAALARAREDLQKMKQFAQDFVMHTDVRTCSSSTSVIADLQEDEDGVYFSSYGHYGIHEEMLKDKIRTESYRDFIYQNPHIFKDKVVLDVGCGTGILSMFAAKAGAKKVLGVDQSEILYQAMDIIRLNKLEDTITLIKGKIEEVHLPVEKVDVIISEWMGYFLLFESMLDSVLYAKNKYLAKGGSVYPDICTISLVAVSDVNKHADRIAFWDDVYGFKMSCMKKAVIPEAVVEVLDPKTLISEPCGIKHIDCHTTSISDLEFSSDFTLKITRTSMCTAIAGYFDIYFEKNCHNRVVFSTGPQSTKTHWKQTVFLLEKPFSVKAGEALKGKVTVHKNKKDPRSLTVTLTLNNSTQTYGLQ