Brand  (β version)

  The number of atoms exceeds 100,000.
  So, it can not be displayed here.

Select unit:

Select hetatm:   

close
information
centroid:
interaction residue:

Select chain:   Sequence  

Data format:   

Color scheme of protein:

Ligands
Code Name Style Show Link
FTG (2s,5s)-2-amino-6-[(2r,3s,4r,5r)-5-(6-amino-9h-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]-5-[(benzylamino)methyl]-N-[2-(4-hydroxyphenyl)ethyl]hexanamide
GOL Glycerol
SO4 Sulfate ion
UNX Unknown atom or ion
Non-standard Residues
Code Name Show
Glycosylation
Code Name Emphasize
Modification
Code Name Show
Code : 6D2L   PDBj   RCSB PDB   PDBe
Header : TRANSFERASE/INHIBITOR
Title : Crystal structure of human CARM1 with (S)-SKI-72
Release Data : 2018-05-23
Compound :
mol_id molecule chains synonym
1 Histone-arginine methyltransferase CARM1 A,B,C,D,E,F Coactivator-associated arginine methyltransferase 1,Protein arginine N-methyltransferase 4
ec: 2.1.1.319
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Spodoptera frugiperda  (taxid:7108)
gene: CARM1, PRMT4
expression_system_strain: Sf9
expression_system_vector_type: plasmid
expression_system_plasmid: pFBOH-MHL
Authors : DONG, A., ZENG, H., WALKER, J.R., Hutchinson, A., Seitova, A., LUO, M., CAI, X.C., KE, W., WANG, J., SHI, C., ZHENG, W., LEE, J.P., IBANEZ, G., Bountra, C., Arrowsmith, C.H., Edwards, A.M., BROWN, P.J., WU, H., Structural Genomics Consortium (SGC)
Keywords : CARM1, PRMT4, SKI-72 inhibitor, Structural Genomics, Structural Genomics Consortium, SGC, TRANSFERASE-INHIBITOR complex
Exp. method : X-RAY DIFFRACTION ( 2.0000 Å )
Citation :

A chemical probe of CARM1 alters epigenetic plasticity against breast cancer cell invasion.

Cai, X.C.,Zhang, T.,Kim, E.J.  et al.
(2019)  Elife  8

PubMed: 31657716
DOI: 10.7554/eLife.47110

Chain : A, B, C, D, E, F
UniProt : Q86X55 (CARM1_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 2.1.1.319 PubMed:19405910
-