5FWA
Crystal Structure of Mus musculus Protein Arginine Methyltransferase 2 with CP1
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 | 19 |
| Details | BINDING SITE FOR RESIDUE J7C A 1446 |
| Chain | Residue |
| A | TYR114 |
| A | VAL208 |
| A | GLU209 |
| A | GLU223 |
| A | TRP224 |
| A | MET225 |
| A | GLU232 |
| A | MET234 |
| A | SER237 |
| A | HOH2018 |
| A | HOH2139 |
| A | PHE115 |
| A | TYR118 |
| A | HIS124 |
| A | GLY157 |
| A | GLU180 |
| A | ALA181 |
| A | SER182 |
| A | LYS207 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PG4 A 1447 |
| Chain | Residue |
| A | ASP150 |
| A | LYS151 |
| A | ASP218 |
| A | ASP249 |
| A | LEU362 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 1448 |
| Chain | Residue |
| A | GLY374 |
| A | PRO375 |
| A | LEU376 |
| A | HIS377 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE EDO A 1449 |
| Chain | Residue |
| A | ARG299 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 1450 |
| Chain | Residue |
| A | PRO375 |
| A | HIS377 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1451 |
| Chain | Residue |
| A | GLN110 |
| A | TYR114 |
| A | PHE231 |
| A | HOH2303 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 1452 |
| Chain | Residue |
| A | GLY196 |
| A | ASP199 |
| A | HOH2087 |
| A | HOH2089 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CA A 1453 |
| Chain | Residue |
| A | HOH2033 |
| A | HOH2033 |
| A | HOH2038 |
| A | HOH2038 |
