Reaction Details Report a problem with these data
Target
Protein arginine N-methyltransferase 5
Ligand
BDBM50595702
Substrate
n/a
Meas. Tech.
ChEMBL_2217502 (CHEMBL5130634)
IC50
1.000000±n/a nM
Citation
Argikar, U; Blatter, M; Bednarczyk, D; Chen, Z; Cho, YS; Doré, M; Dumouchel, JL; Ho, S; Hoegenauer, K; Kawanami, T; Mathieu, S; Meredith, E; Möbitz, H; Murphy, SK; Parthasarathy, S; Soldermann, CP; Santos, J; Silver, S; Skolnik, S; Stojanovic, A Paradoxical Increase of Permeability and Lipophilicity with the Increasing Topological Polar Surface Area within a Series of PRMT5 Inhibitors. J Med Chem 65:12386-12402 (2022) [PubMed]
More Info.:
Target
Name:
Protein arginine N-methyltransferase 5
Synonyms:
72 kDa ICln-binding protein | ANM5_HUMAN | HRMT1L5 | Histone-arginine N-methyltransferase PRMT5 | IBP72 | JBP1 | Jak-binding protein 1 | PRMT5 | PRMT5/MEP50 complex | Protein arginine N-methyltransferase 5 (PRMT5) | Protein arginine methyltransferase 5 (PRMT5) | SKB1 | SKB1 homolog | SKB1Hs | Shk1 kinase-binding protein 1 homolog
Type:
Enzyme
Mol. Mass.:
72679.99
Organism:
Homo sapiens (Human)
Description:
O14744
Residue:
637
Sequence:
MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFIQEPAKNRPGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLPAFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTTHTEEYSGEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNKKGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELFAKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNVQVLMVLGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDMREWVAPEKADIIVSELLGSFADNELSPECLDGAQHFLKDDGVSIPGEYTSFLAPISSSKLYNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEFPVEVNTVLHGFAGYFETVLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICVRFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRSYTIGL