2Y1X
CRYSTAL STRUCTURE OF COACTIVATOR ASSOCIATED ARGININE METHYLTRANSFERASE 1 (CARM1) IN COMPLEX WITH SINEFUNGIN AND INDOLE INHIBITOR
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 | 23 |
| Details | BINDING SITE FOR RESIDUE SAH A 1001 |
| Chain | Residue |
| A | PHE151 |
| A | LEU199 |
| A | GLU215 |
| A | ALA216 |
| A | GLY241 |
| A | LYS242 |
| A | VAL243 |
| A | GLU244 |
| A | GLU258 |
| A | MET269 |
| A | SER272 |
| A | TYR154 |
| A | 8451002 |
| A | HOH2019 |
| A | HOH2122 |
| A | HOH2123 |
| A | GLN160 |
| A | MET163 |
| A | ARG169 |
| A | GLY193 |
| A | CYS194 |
| A | GLY195 |
| A | ILE198 |
| site_id | AC2 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE SAH B 1001 |
| Chain | Residue |
| 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 | 8451002 |
| B | HOH2006 |
| B | HOH2015 |
| B | HOH2016 |
| B | HOH2035 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE SAH C 1001 |
| Chain | Residue |
| C | TYR150 |
| C | PHE151 |
| C | TYR154 |
| C | GLN160 |
| C | MET163 |
| C | ARG169 |
| C | GLY193 |
| C | CYS194 |
| C | GLY195 |
| C | ILE198 |
| C | LEU199 |
| C | GLU215 |
| C | ALA216 |
| C | GLY241 |
| C | LYS242 |
| C | VAL243 |
| C | GLU244 |
| C | GLU258 |
| C | MET269 |
| C | SER272 |
| C | 8451002 |
| C | HOH2027 |
| C | HOH2136 |
| C | HOH2137 |
| site_id | AC4 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE SAH D 1001 |
| Chain | Residue |
| 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 | 8451002 |
| D | HOH2020 |
| D | HOH2021 |
| D | HOH2022 |
| D | HOH2112 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE 845 A 1002 |
| Chain | Residue |
| A | GLU258 |
| A | MET260 |
| A | TYR262 |
| A | ASN266 |
| A | GLU267 |
| A | HIS415 |
| A | TRP416 |
| A | TYR417 |
| A | PHE475 |
| A | TYR477 |
| A | SAH1001 |
| A | HOH2029 |
| A | HOH2124 |
| A | PHE153 |
| A | TYR154 |
| A | GLN159 |
| A | ASN162 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE 845 B 1002 |
| Chain | Residue |
| B | PHE153 |
| B | TYR154 |
| B | GLN159 |
| B | ASN162 |
| B | GLU258 |
| B | PRO259 |
| B | MET260 |
| B | TYR262 |
| B | ASN266 |
| B | GLU267 |
| B | HIS415 |
| B | TRP416 |
| B | PHE475 |
| B | TYR477 |
| B | SAH1001 |
| B | HOH2086 |
| site_id | AC7 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 845 C 1002 |
| Chain | Residue |
| C | TYR154 |
| C | GLN159 |
| C | ASN162 |
| C | MET163 |
| C | GLU258 |
| C | MET260 |
| C | TYR262 |
| C | ASN266 |
| C | GLU267 |
| C | HIS415 |
| C | TRP416 |
| C | TYR417 |
| C | PHE475 |
| C | TYR477 |
| C | SAH1001 |
| site_id | AC8 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE 845 D 1002 |
| Chain | Residue |
| D | PHE153 |
| D | TYR154 |
| D | GLN159 |
| D | ASN162 |
| D | GLU258 |
| D | MET260 |
| D | TYR262 |
| D | GLU267 |
| D | HIS415 |
| D | TRP416 |
| D | PHE475 |
| D | SAH1001 |
| D | HOH2039 |
| D | HOH2113 |
| site_id | AC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 1003 |
| Chain | Residue |
| A | GLN149 |
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":"UniProtKB","id":"Q9WVG6","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21410432","evidenceCode":"ECO:0000305"}]} |
| 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":"PubMed","id":"34480022","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
