5K8W
Crystal structure of mouse CARM1 in complex with inhibitor U2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
| A | 0018216 | biological_process | peptidyl-arginine methylation |
| B | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
| B | 0018216 | biological_process | peptidyl-arginine methylation |
| C | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
| C | 0018216 | biological_process | peptidyl-arginine methylation |
| D | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
| D | 0018216 | biological_process | peptidyl-arginine methylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 18 |
| Details | binding site for residue GJV A 501 |
| Chain | Residue |
| A | TYR150 |
| A | GLU244 |
| A | GLU258 |
| A | MET260 |
| A | GLU267 |
| A | MET269 |
| A | SER272 |
| A | HOH657 |
| A | HOH679 |
| A | HOH697 |
| A | PHE151 |
| A | TYR154 |
| A | GLY193 |
| A | GLU215 |
| A | ALA216 |
| A | GLY241 |
| A | LYS242 |
| A | VAL243 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue DXE A 502 |
| Chain | Residue |
| A | GLN149 |
| A | GLU267 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue DXE A 503 |
| Chain | Residue |
| A | LEU178 |
| A | HOH688 |
| D | ASP458 |
| D | GLY461 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | HOH780 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | GLU411 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | LEU413 |
| A | THR414 |
| A | HIS415 |
| A | TYR417 |
| A | HOH670 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue PG4 A 507 |
| Chain | Residue |
| A | LYS463 |
| B | SER136 |
| B | GLU244 |
| B | GLU245 |
| B | VAL246 |
| B | LYS278 |
| B | HOH623 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 508 |
| Chain | Residue |
| A | SER283 |
| A | GLY284 |
| A | GLY398 |
| A | SER399 |
| site_id | AC9 |
| Number of Residues | 19 |
| Details | binding site for residue GJV B 501 |
| Chain | Residue |
| B | PHE138 |
| B | TYR150 |
| B | PHE151 |
| B | TYR154 |
| B | GLY193 |
| B | GLU215 |
| B | ALA216 |
| B | GLY241 |
| B | LYS242 |
| B | VAL243 |
| B | GLU244 |
| B | GLU258 |
| B | MET260 |
| B | GLU267 |
| B | MET269 |
| B | SER272 |
| B | HOH619 |
| B | HOH705 |
| B | HOH706 |
| site_id | AD1 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| B | THR460 |
| B | GLY461 |
| B | HOH643 |
| C | LEU178 |
| C | GLN205 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| B | TYR150 |
| B | HOH685 |
| B | HOH753 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue PEG B 504 |
| Chain | Residue |
| B | TRP404 |
| B | HOH625 |
| site_id | AD4 |
| Number of Residues | 17 |
| Details | binding site for residue GJV C 501 |
| Chain | Residue |
| C | PHE151 |
| C | TYR154 |
| C | GLN160 |
| C | GLY193 |
| C | GLU215 |
| C | ALA216 |
| C | GLY241 |
| C | LYS242 |
| C | VAL243 |
| C | GLU244 |
| C | GLU258 |
| C | PRO259 |
| C | MET260 |
| C | GLU267 |
| C | MET269 |
| C | SER272 |
| C | HOH737 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue DXE C 502 |
| Chain | Residue |
| C | TYR150 |
| C | PHE153 |
| C | GLU267 |
| site_id | AD6 |
| Number of Residues | 1 |
| Details | binding site for residue DXE C 503 |
| Chain | Residue |
| C | TRP404 |
| site_id | AD7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 504 |
| Chain | Residue |
| C | LYS277 |
| C | LEU280 |
| C | HOH632 |
| site_id | AD8 |
| Number of Residues | 1 |
| Details | binding site for residue EDO C 505 |
| Chain | Residue |
| C | TYR417 |
| site_id | AD9 |
| Number of Residues | 1 |
| Details | binding site for residue EDO C 506 |
| Chain | Residue |
| C | GLU411 |
| site_id | AE1 |
| Number of Residues | 3 |
| Details | binding site for residue DXE C 507 |
| Chain | Residue |
| C | HOH774 |
| C | GLY398 |
| C | SER399 |
| site_id | AE2 |
| Number of Residues | 18 |
| Details | binding site for residue GJV D 501 |
| Chain | Residue |
| D | TYR150 |
| D | PHE151 |
| D | TYR154 |
| D | GLY193 |
| D | GLU215 |
| D | ALA216 |
| D | GLY241 |
| D | LYS242 |
| D | VAL243 |
| D | GLU244 |
| D | GLU258 |
| D | MET260 |
| D | GLU267 |
| D | MET269 |
| D | SER272 |
| D | HOH647 |
| D | HOH722 |
| D | HOH734 |
| site_id | AE3 |
| Number of Residues | 2 |
| Details | binding site for residue DXE D 502 |
| Chain | Residue |
| D | ASP393 |
| D | TRP404 |
| site_id | AE4 |
| Number of Residues | 1 |
| Details | binding site for residue EDO D 503 |
| Chain | Residue |
| D | GLN149 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17882261 |
| Chain | Residue | Details |
| A | GLN160 | |
| B | GLU215 | |
| B | GLU244 | |
| B | SER272 | |
| C | GLN160 | |
| C | ARG169 | |
| C | GLY193 | |
| C | GLU215 | |
| C | GLU244 | |
| C | SER272 | |
| D | GLN160 | |
| A | ARG169 | |
| D | ARG169 | |
| D | GLY193 | |
| D | GLU215 | |
| D | GLU244 | |
| D | SER272 | |
| A | GLY193 | |
| A | GLU215 | |
| A | GLU244 | |
| A | SER272 | |
| B | GLN160 | |
| B | ARG169 | |
| B | GLY193 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:19843527 |
| Chain | Residue | Details |
| A | SER217 | |
| B | SER217 | |
| C | SER217 | |
| D | SER217 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q86X55 |
| Chain | Residue | Details |
| A | LYS228 | |
| B | LYS228 | |
| C | LYS228 | |
| D | LYS228 |
