5LGQ
Crystal structure of mouse CARM1 in complex with ligand P2C3s
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 | 1 |
| Details | binding site for residue EDO A 501 |
| Chain | Residue |
| A | GLY398 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue PEG A 502 |
| Chain | Residue |
| A | TRP404 |
| A | HOH638 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue PEG A 503 |
| Chain | Residue |
| D | THR460 |
| A | GLN174 |
| A | LEU178 |
| A | GLN205 |
| A | HOH689 |
| A | HOH804 |
| D | ASP458 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue DXE A 504 |
| Chain | Residue |
| A | TYR315 |
| A | TYR315 |
| A | SER325 |
| A | ARG328 |
| A | GLY329 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue PG6 A 505 |
| Chain | Residue |
| A | GLN456 |
| A | LYS463 |
| A | SER465 |
| B | GLU244 |
| B | GLU245 |
| B | VAL246 |
| B | SER247 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 506 |
| Chain | Residue |
| A | ASN444 |
| A | LYS445 |
| A | HOH612 |
| B | ARG209 |
| site_id | AC7 |
| Number of Residues | 1 |
| Details | binding site for residue EDO B 501 |
| Chain | Residue |
| B | HOH601 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| B | TYR356 |
| B | ALA363 |
| B | HOH608 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 503 |
| Chain | Residue |
| B | PRO409 |
| B | GLU411 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 501 |
| Chain | Residue |
| C | ASP393 |
| C | TRP404 |
| C | HOH679 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO C 502 |
| Chain | Residue |
| C | VAL332 |
| C | ASP333 |
| C | GLN424 |
| C | HOH633 |
| site_id | AD3 |
| Number of Residues | 4 |
| Details | binding site for residue PEG C 503 |
| Chain | Residue |
| C | TYR315 |
| C | ARG328 |
| C | VAL332 |
| C | HOH619 |
| site_id | AD4 |
| Number of Residues | 1 |
| Details | binding site for residue EDO D 501 |
| Chain | Residue |
| D | TRP404 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue PEG D 502 |
| Chain | Residue |
| B | SER325 |
| B | ARG328 |
| D | ARG328 |
| site_id | AD6 |
| Number of Residues | 25 |
| Details | binding site for Di-peptide QVR E 101 and ARG E 1 |
| Chain | Residue |
| A | TYR150 |
| A | PHE151 |
| A | TYR154 |
| A | MET163 |
| A | GLY193 |
| A | GLU215 |
| A | ALA216 |
| A | GLY241 |
| A | LYS242 |
| A | VAL243 |
| A | GLU244 |
| A | GLU258 |
| A | MET260 |
| A | GLU267 |
| A | MET269 |
| A | SER272 |
| A | HIS415 |
| A | HOH628 |
| A | HOH644 |
| E | ALA-1 |
| E | PRO0 |
| E | PRO2 |
| E | PRO3 |
| E | HOH203 |
| E | HOH205 |
| site_id | AD7 |
| Number of Residues | 25 |
| Details | binding site for Di-peptide QVR F 101 and ARG F 1 |
| Chain | Residue |
| B | PHE138 |
| B | TYR150 |
| B | PHE151 |
| B | TYR154 |
| B | MET163 |
| B | GLY193 |
| B | GLU215 |
| B | ALA216 |
| B | GLY241 |
| B | LYS242 |
| B | VAL243 |
| B | GLU244 |
| B | GLU258 |
| B | GLU267 |
| B | MET269 |
| B | SER272 |
| B | HIS415 |
| B | HOH651 |
| B | HOH673 |
| F | ALA-1 |
| F | PRO0 |
| F | PRO2 |
| F | PRO3 |
| F | HOH201 |
| F | HOH204 |
| site_id | AD8 |
| Number of Residues | 25 |
| Details | binding site for Di-peptide QVR G 101 and ARG G 1 |
| Chain | Residue |
| C | TYR154 |
| C | MET163 |
| C | GLY193 |
| C | GLU215 |
| C | ALA216 |
| C | GLY241 |
| C | LYS242 |
| C | VAL243 |
| C | GLU244 |
| C | GLU258 |
| C | MET260 |
| C | GLU267 |
| C | MET269 |
| C | SER272 |
| C | HIS415 |
| C | TRP416 |
| C | HOH632 |
| G | ALA-1 |
| G | PRO0 |
| G | PRO2 |
| G | PRO3 |
| G | HOH201 |
| G | HOH203 |
| C | TYR150 |
| C | PHE151 |
| site_id | AD9 |
| Number of Residues | 25 |
| Details | binding site for Di-peptide QVR H 101 and ARG H 1 |
| Chain | Residue |
| D | PHE138 |
| D | TYR150 |
| D | PHE151 |
| D | TYR154 |
| D | MET163 |
| 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 | HIS415 |
| H | ALA-1 |
| H | PRO0 |
| H | PRO2 |
| H | PRO3 |
| H | HOH203 |
| H | HOH204 |
| H | HOH205 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | MOD_RES: Omega-N-methylated arginine; by CARM1; partial => ECO:0000305|PubMed:11850402 |
| Chain | Residue | Details |
| F | ARG1 | |
| B | GLU215 | |
| B | GLU244 | |
| B | SER272 | |
| C | GLN160 | |
| C | ARG169 | |
| C | GLY193 | |
| C | GLU215 | |
| C | GLU244 | |
| C | SER272 | |
| D | GLN160 | |
| E | ARG1 | |
| D | ARG169 | |
| D | GLY193 | |
| D | GLU215 | |
| D | GLU244 | |
| D | SER272 | |
| G | ARG1 | |
| H | ARG1 | |
| 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 |
