5JMQ
Crystal Structure of Mus musculus Protein Arginine Methyltransferase 2 with CP3
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003713 | molecular_function | transcription coactivator activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005654 | cellular_component | nucleoplasm |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
| A | 0018216 | biological_process | peptidyl-arginine methylation |
| A | 0030331 | molecular_function | nuclear estrogen receptor binding |
| A | 0033142 | molecular_function | nuclear progesterone receptor binding |
| A | 0035242 | molecular_function | protein-arginine omega-N asymmetric methyltransferase activity |
| A | 0042054 | molecular_function | histone methyltransferase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0042974 | molecular_function | nuclear retinoic acid receptor binding |
| A | 0042975 | molecular_function | peroxisome proliferator activated receptor binding |
| A | 0043124 | biological_process | negative regulation of canonical NF-kappaB signal transduction |
| A | 0045893 | biological_process | positive regulation of DNA-templated transcription |
| A | 0046966 | molecular_function | nuclear thyroid hormone receptor binding |
| A | 0050681 | molecular_function | nuclear androgen receptor binding |
| A | 0050728 | biological_process | negative regulation of inflammatory response |
| A | 0060765 | biological_process | regulation of androgen receptor signaling pathway |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue PG4 A 501 |
| Chain | Residue |
| A | LYS151 |
| A | ASP218 |
| A | ASP249 |
| A | LEU362 |
| site_id | AC2 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | HIS377 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 503 |
| Chain | Residue |
| A | EDO505 |
| A | GLN110 |
| A | TYR114 |
| A | GLU232 |
| A | ARG415 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | ARG299 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | GLN110 |
| A | GLU113 |
| A | HIS416 |
| A | TRP445 |
| A | EDO503 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue CA A 506 |
| Chain | Residue |
| A | GLY196 |
| A | ASP199 |
| A | HOH686 |
| A | HOH773 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue CL A 507 |
| Chain | Residue |
| A | GLY374 |
| A | PRO375 |
| A | LEU376 |
| A | HIS377 |
| A | HOH918 |
| site_id | AC8 |
| Number of Residues | 18 |
| Details | binding site for residue 6LC A 508 |
| Chain | Residue |
| A | PHE115 |
| A | TYR118 |
| A | HIS124 |
| A | MET127 |
| A | GLY157 |
| A | GLU180 |
| A | ALA181 |
| A | GLN206 |
| A | LYS207 |
| A | VAL208 |
| A | GLU209 |
| A | GLU223 |
| A | MET225 |
| A | MET234 |
| A | SER237 |
| A | HIS381 |
| A | TRP382 |
| A | HOH749 |
