5IS9
Crystal structure of mouse CARM1 in complex with inhibitor SA0375
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 | 31 |
Details | binding site for residue 6D3 A 501 |
Chain | Residue |
A | TYR150 |
A | LEU199 |
A | GLU215 |
A | ALA216 |
A | GLY241 |
A | LYS242 |
A | VAL243 |
A | GLU244 |
A | GLU258 |
A | MET260 |
A | GLY261 |
A | PHE151 |
A | TYR262 |
A | ASN266 |
A | GLU267 |
A | MET269 |
A | SER272 |
A | HIS415 |
A | TRP416 |
A | EDO502 |
A | HOH615 |
A | HOH651 |
A | TYR154 |
A | HOH656 |
A | HOH672 |
A | GLN160 |
A | MET163 |
A | ARG169 |
A | GLY193 |
A | CYS194 |
A | ILE198 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue EDO A 502 |
Chain | Residue |
A | PHE153 |
A | 6D3501 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | HOH632 |
site_id | AC4 |
Number of Residues | 4 |
Details | binding site for residue EDO A 504 |
Chain | Residue |
A | LEU413 |
A | HIS415 |
A | TYR417 |
A | HOH620 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue EDO A 505 |
Chain | Residue |
A | LYS242 |
A | HOH635 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue EDO A 506 |
Chain | Residue |
A | TYR315 |
A | GLN316 |
A | PRO317 |
A | ARG328 |
site_id | AC7 |
Number of Residues | 2 |
Details | binding site for residue PEG A 507 |
Chain | Residue |
A | LEU178 |
D | GLY461 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue PEG A 508 |
Chain | Residue |
A | PRO317 |
A | VAL332 |
A | ASP333 |
A | GLN424 |
A | SER425 |
site_id | AC9 |
Number of Residues | 1 |
Details | binding site for residue DXE A 509 |
Chain | Residue |
A | GLY398 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue DXE A 510 |
Chain | Residue |
A | PG4511 |
B | TYR279 |
site_id | AD2 |
Number of Residues | 5 |
Details | binding site for residue PG4 A 511 |
Chain | Residue |
A | LYS463 |
A | DXE510 |
B | SER136 |
B | GLU244 |
B | GLU245 |
site_id | AD3 |
Number of Residues | 27 |
Details | binding site for residue 6D3 B 501 |
Chain | Residue |
B | TYR150 |
B | PHE151 |
B | TYR154 |
B | GLN160 |
B | ARG169 |
B | GLY193 |
B | CYS194 |
B | ILE198 |
B | LEU199 |
B | GLU215 |
B | ALA216 |
B | GLY241 |
B | LYS242 |
B | VAL243 |
B | GLU244 |
B | GLU258 |
B | MET260 |
B | GLY261 |
B | TYR262 |
B | ASN266 |
B | GLU267 |
B | MET269 |
B | SER272 |
B | HIS415 |
B | EDO502 |
B | HOH632 |
B | HOH641 |
site_id | AD4 |
Number of Residues | 2 |
Details | binding site for residue EDO B 502 |
Chain | Residue |
B | 6D3501 |
B | HOH628 |
site_id | AD5 |
Number of Residues | 1 |
Details | binding site for residue EDO B 503 |
Chain | Residue |
B | TYR417 |
site_id | AD6 |
Number of Residues | 1 |
Details | binding site for residue EDO B 504 |
Chain | Residue |
B | LYS277 |
site_id | AD7 |
Number of Residues | 2 |
Details | binding site for residue PEG B 505 |
Chain | Residue |
B | ASP393 |
B | TRP404 |
site_id | AD8 |
Number of Residues | 7 |
Details | binding site for residue M2M B 506 |
Chain | Residue |
B | ASP333 |
B | GLN424 |
B | SER452 |
B | SER465 |
B | ASN466 |
B | LEU467 |
B | HOH697 |
site_id | AD9 |
Number of Residues | 29 |
Details | binding site for residue 6D3 C 501 |
Chain | Residue |
C | TYR150 |
C | PHE151 |
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 | MET260 |
C | TYR262 |
C | GLU267 |
C | MET269 |
C | SER272 |
C | HIS415 |
C | TRP416 |
C | HOH615 |
C | HOH623 |
C | HOH629 |
C | HOH639 |
C | HOH670 |
site_id | AE1 |
Number of Residues | 3 |
Details | binding site for residue EDO C 502 |
Chain | Residue |
C | GLN149 |
C | PHE153 |
C | HOH623 |
site_id | AE2 |
Number of Residues | 2 |
Details | binding site for residue EDO C 503 |
Chain | Residue |
C | TRP404 |
C | HOH638 |
site_id | AE3 |
Number of Residues | 2 |
Details | binding site for residue EDO C 504 |
Chain | Residue |
C | LEU178 |
C | GLN205 |
site_id | AE4 |
Number of Residues | 1 |
Details | binding site for residue EDO C 506 |
Chain | Residue |
C | HIS415 |
site_id | AE5 |
Number of Residues | 28 |
Details | binding site for residue 6D3 D 501 |
Chain | Residue |
D | TYR150 |
D | PHE151 |
D | TYR154 |
D | GLN160 |
D | MET163 |
D | ARG169 |
D | GLY193 |
D | CYS194 |
D | ILE198 |
D | LEU199 |
D | GLU215 |
D | ALA216 |
D | GLY241 |
D | LYS242 |
D | VAL243 |
D | GLU244 |
D | GLU258 |
D | MET260 |
D | GLY261 |
D | TYR262 |
D | ASN266 |
D | GLU267 |
D | MET269 |
D | SER272 |
D | HIS415 |
D | EDO504 |
D | HOH626 |
D | HOH651 |
site_id | AE6 |
Number of Residues | 1 |
Details | binding site for residue EDO D 502 |
Chain | Residue |
D | TRP404 |
site_id | AE7 |
Number of Residues | 5 |
Details | binding site for residue EDO D 503 |
Chain | Residue |
D | ASP333 |
D | GLN424 |
D | ASN466 |
D | LEU467 |
D | PEG505 |
site_id | AE8 |
Number of Residues | 2 |
Details | binding site for residue EDO D 504 |
Chain | Residue |
D | GLN149 |
D | 6D3501 |
site_id | AE9 |
Number of Residues | 3 |
Details | binding site for residue PEG D 505 |
Chain | Residue |
D | GLN424 |
D | SER465 |
D | EDO503 |
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 |