5TBH
Crystal structure of mouse CARM1 in complex with inhibitor LH1236
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 | 4 |
| Details | binding site for residue M2M A 501 |
| Chain | Residue |
| A | PHE153 |
| A | TYR262 |
| A | GLU267 |
| A | EDO506 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | ALA330 |
| A | ASP333 |
| A | GLU334 |
| A | ARG337 |
| A | HOH604 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue PG4 A 504 |
| Chain | Residue |
| A | LEU178 |
| A | GLN205 |
| D | ASP458 |
| D | GLY461 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | binding site for residue EDO A 505 |
| Chain | Residue |
| A | TRP404 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue EDO A 506 |
| Chain | Residue |
| A | GLU258 |
| A | MET260 |
| A | GLU267 |
| A | HIS415 |
| A | TRP416 |
| A | M2M501 |
| site_id | AC6 |
| Number of Residues | 21 |
| Details | binding site for residue SAO A 507 |
| Chain | Residue |
| A | TYR150 |
| A | PHE151 |
| A | TYR154 |
| A | GLN160 |
| A | MET163 |
| A | ARG169 |
| A | GLY193 |
| A | CYS194 |
| A | ILE198 |
| A | LEU199 |
| A | GLU215 |
| A | ALA216 |
| A | GLY241 |
| A | LYS242 |
| A | VAL243 |
| A | GLU244 |
| A | MET269 |
| A | SER272 |
| A | HOH607 |
| A | HOH645 |
| A | HOH660 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 501 |
| Chain | Residue |
| A | LYS463 |
| B | GLU244 |
| B | GLU245 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 502 |
| Chain | Residue |
| A | LYS463 |
| B | GLU245 |
| B | HOH619 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 505 |
| Chain | Residue |
| B | PHE153 |
| B | TYR154 |
| B | GLU267 |
| site_id | AD1 |
| Number of Residues | 27 |
| Details | binding site for residue 78K B 506 |
| Chain | Residue |
| B | TYR150 |
| B | PHE151 |
| B | TYR154 |
| B | GLN159 |
| B | GLN160 |
| B | MET163 |
| B | GLY193 |
| B | CYS194 |
| B | GLY195 |
| B | ILE198 |
| B | LEU199 |
| B | GLU215 |
| B | ALA216 |
| B | GLY241 |
| B | LYS242 |
| B | VAL243 |
| B | GLU244 |
| B | GLU258 |
| B | PRO259 |
| B | MET260 |
| B | GLY261 |
| B | GLU267 |
| B | MET269 |
| B | SER272 |
| B | HIS415 |
| B | TRP416 |
| B | HOH654 |
| site_id | AD2 |
| Number of Residues | 1 |
| Details | binding site for residue EDO C 501 |
| Chain | Residue |
| C | TYR417 |
| site_id | AD3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 502 |
| Chain | Residue |
| C | LYS277 |
| C | LEU280 |
| C | LYS281 |
| site_id | AD4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO C 503 |
| Chain | Residue |
| C | TYR154 |
| C | MET163 |
| C | GLU258 |
| C | MET260 |
| C | HIS415 |
| C | TRP416 |
| C | SAO506 |
| site_id | AD5 |
| Number of Residues | 1 |
| Details | binding site for residue EDO C 504 |
| Chain | Residue |
| C | PHE153 |
| site_id | AD6 |
| Number of Residues | 2 |
| Details | binding site for residue EDO C 505 |
| Chain | Residue |
| C | ASP393 |
| C | TRP404 |
| site_id | AD7 |
| Number of Residues | 24 |
| Details | binding site for residue SAO C 506 |
| Chain | Residue |
| C | ILE198 |
| C | LEU199 |
| C | GLU215 |
| C | ALA216 |
| C | GLY241 |
| C | LYS242 |
| C | VAL243 |
| C | GLU244 |
| C | GLU258 |
| C | MET269 |
| C | SER272 |
| C | EDO503 |
| C | HOH613 |
| C | HOH618 |
| C | HOH620 |
| C | HOH641 |
| C | TYR150 |
| C | PHE151 |
| C | TYR154 |
| C | GLN160 |
| C | MET163 |
| C | ARG169 |
| C | GLY193 |
| C | CYS194 |
| site_id | AD8 |
| Number of Residues | 1 |
| Details | binding site for residue EDO D 502 |
| Chain | Residue |
| D | HOH614 |
| site_id | AD9 |
| Number of Residues | 1 |
| Details | binding site for residue EDO D 503 |
| Chain | Residue |
| D | ARG476 |
| site_id | AE1 |
| Number of Residues | 24 |
| Details | binding site for residue 78K D 504 |
| Chain | Residue |
| D | TYR150 |
| D | PHE151 |
| D | TYR154 |
| D | MET163 |
| D | ARG169 |
| D | GLY193 |
| D | CYS194 |
| D | GLY195 |
| D | ILE198 |
| D | GLU215 |
| D | ALA216 |
| D | LYS242 |
| D | VAL243 |
| D | GLU244 |
| D | GLU258 |
| D | PRO259 |
| D | MET260 |
| D | GLY261 |
| D | GLU267 |
| D | MET269 |
| D | SER272 |
| D | HIS415 |
| D | TRP416 |
| D | HOH637 |
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 |
