5IS6
Crystal structure of mouse CARM1 in complex with Sinefungin at 2.0 Angstroms resolution
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 | 11 |
| Details | binding site for residue PG4 A 501 |
| Chain | Residue |
| A | GLN149 |
| A | HOH614 |
| A | HOH739 |
| A | PHE153 |
| A | TYR154 |
| A | MET260 |
| A | TYR262 |
| A | GLU267 |
| A | HIS415 |
| A | TRP416 |
| A | HOH601 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 502 |
| Chain | Residue |
| A | LEU178 |
| A | HOH756 |
| D | ASP458 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 503 |
| Chain | Residue |
| A | GLY284 |
| A | ASN285 |
| A | GLY398 |
| A | SER399 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue PEG A 504 |
| Chain | Residue |
| A | PRO317 |
| A | VAL332 |
| A | GLN424 |
| A | SER425 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue DXE A 506 |
| Chain | Residue |
| A | HOH672 |
| A | HOH800 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | binding site for residue SFG 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 | GLU258 |
| A | MET269 |
| A | SER272 |
| A | HOH620 |
| A | HOH630 |
| A | HOH705 |
| A | HOH721 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | binding site for residue PG4 B 2001 |
| Chain | Residue |
| A | LYS463 |
| B | SER136 |
| B | GLU244 |
| B | GLU245 |
| B | HOH2169 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 2003 |
| Chain | Residue |
| B | ALA147 |
| B | PHE151 |
| B | LYS242 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | binding site for residue DXE B 2004 |
| Chain | Residue |
| B | TYR154 |
| site_id | AD1 |
| Number of Residues | 1 |
| Details | binding site for residue DXE B 2005 |
| Chain | Residue |
| B | HOH2317 |
| site_id | AD2 |
| Number of Residues | 24 |
| Details | binding site for residue SFG B 2006 |
| Chain | Residue |
| B | TYR150 |
| B | PHE151 |
| B | TYR154 |
| B | GLN160 |
| B | MET163 |
| B | ARG169 |
| 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 | MET269 |
| B | SER272 |
| B | HOH2136 |
| B | HOH2141 |
| B | HOH2171 |
| B | HOH2195 |
| site_id | AD3 |
| Number of Residues | 10 |
| Details | binding site for residue PG4 C 501 |
| Chain | Residue |
| C | GLN149 |
| C | TYR154 |
| C | MET260 |
| C | TYR262 |
| C | GLU267 |
| C | HIS415 |
| C | TRP416 |
| C | HOH602 |
| C | HOH676 |
| C | HOH713 |
| site_id | AD4 |
| Number of Residues | 2 |
| Details | binding site for residue EDO C 503 |
| Chain | Residue |
| C | HOH601 |
| C | HOH807 |
| site_id | AD5 |
| Number of Residues | 2 |
| Details | binding site for residue EDO C 504 |
| Chain | Residue |
| C | LEU178 |
| C | GLN205 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue PEG C 505 |
| Chain | Residue |
| C | HOH769 |
| C | LYS277 |
| C | LEU280 |
| C | LEU361 |
| C | HOH746 |
| site_id | AD7 |
| Number of Residues | 2 |
| Details | binding site for residue DXE C 506 |
| Chain | Residue |
| C | VAL332 |
| C | GLN424 |
| site_id | AD8 |
| Number of Residues | 22 |
| Details | binding site for residue SFG C 507 |
| Chain | Residue |
| C | TYR150 |
| C | TYR154 |
| C | GLN160 |
| C | MET163 |
| C | ARG169 |
| C | GLY193 |
| C | CYS194 |
| C | ILE198 |
| C | LEU199 |
| C | GLU215 |
| C | ALA216 |
| C | GLY241 |
| C | LYS242 |
| C | VAL243 |
| C | GLU244 |
| C | GLU258 |
| C | MET269 |
| C | SER272 |
| C | HOH645 |
| C | HOH665 |
| C | HOH689 |
| C | HOH737 |
| site_id | AD9 |
| Number of Residues | 1 |
| Details | binding site for residue EDO D 501 |
| Chain | Residue |
| D | GLN149 |
| site_id | AE1 |
| Number of Residues | 2 |
| Details | binding site for residue DXE D 503 |
| Chain | Residue |
| D | ASP393 |
| D | TRP404 |
| site_id | AE2 |
| Number of Residues | 24 |
| Details | binding site for residue SFG D 504 |
| Chain | Residue |
| D | TYR150 |
| D | PHE151 |
| D | TYR154 |
| D | GLN160 |
| D | MET163 |
| D | ARG169 |
| D | GLY193 |
| D | CYS194 |
| D | GLY195 |
| D | ILE198 |
| D | LEU199 |
| D | GLU215 |
| D | ALA216 |
| D | GLY241 |
| D | LYS242 |
| D | VAL243 |
| D | GLU244 |
| D | GLU258 |
| D | MET269 |
| D | SER272 |
| D | HOH637 |
| D | HOH649 |
| D | HOH704 |
| D | HOH708 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1228 |
| Details | Domain: {"description":"SAM-dependent MTase PRMT-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01015","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 132 |
| Details | Region: {"description":"Required for nuclear translocation","evidences":[{"source":"PubMed","id":"30366907","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17882261","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19843527","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"Q86X55","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
