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Ligands
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F5J 7-[(5r)-5-C-phenyl-beta-D-ribofuranosyl]-7h-pyrrolo[2,3-D]pyrimidin-4-amine
Non-standard Residues
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Glycosylation
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Code : 6CKC   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE
Title : Structure of PRMT5:MEP50 in complex with LLY-283, a potent and selective inhibitor of PRMT5, with antitumor activity
Release Data : 2018-05-16
Compound :
mol_id molecule chains synonym
1 Protein arginine N-methyltransferase 5 A 72 kDa ICln-binding protein,Histone-arginine N-methyltransferase PRMT5,Jak-binding protein 1,Shk1 kinase-binding protein 1 homolog,SKB1Hs
ec: 2.1.1.320
mol_id molecule chains synonym
2 Methylosome protein 50 B MEP-50,Androgen receptor cofactor p44,WD repeat-containing protein 77,p44/Mep50
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Spodoptera frugiperda  (taxid:7108)
gene: PRMT5, HRMT1L5, IBP72, JBP1, SKB1
mol_id organism_scientific organism_common expression_system
2 Homo sapiens  (taxid:9606) Human Spodoptera frugiperda  (taxid:7108)
gene: WDR77, MEP50, WD45, HKMT1069, Nbla10071
Authors : Antonysamy, S.
Keywords : Inhibitor, Complex, TRANSFERASE
Exp. method : X-RAY DIFFRACTION ( 2.8000 Å )
Citation :

LLY-283, a Potent and Selective Inhibitor of Arginine Methyltransferase 5, PRMT5, with Antitumor Activity.

Bonday, Z.Q.,Cortez, G.S.,Grogan, M.J.  et al.
(2018)  ACS Med Chem Lett  9 : 612 - 617

PubMed: 30034588
DOI: 10.1021/acsmedchemlett.8b00014

Chain : A
UniProt : O14744 (ANM5_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L- homocysteine 2.1.1.320 PubMed:19011621, PubMed:21081503, PubMed:23071334
-
Chain : B
UniProt : Q9BQA1 (MEP50_HUMAN)
Reaction : -