5ISC
Crystal structure of mouse CARM1 in complex with inhibitor SA0491
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 | 12 |
Details | binding site for residue SAO A 501 |
Chain | Residue |
A | ARG169 |
A | VAL243 |
A | GLU244 |
A | MET269 |
A | GLY193 |
A | CYS194 |
A | ILE198 |
A | LEU199 |
A | GLU215 |
A | ALA216 |
A | GLY241 |
A | LYS242 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue EDO A 502 |
Chain | Residue |
A | LYS277 |
A | PRO282 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | TRP404 |
site_id | AC4 |
Number of Residues | 16 |
Details | binding site for residue 6D0 B 501 |
Chain | Residue |
B | PHE151 |
B | TYR154 |
B | GLN160 |
B | MET163 |
B | ARG169 |
B | GLY193 |
B | CYS194 |
B | ILE198 |
B | GLU215 |
B | ALA216 |
B | LYS242 |
B | VAL243 |
B | GLU244 |
B | GLU258 |
B | MET260 |
B | SER272 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue EDO B 502 |
Chain | Residue |
B | TRP404 |
site_id | AC6 |
Number of Residues | 11 |
Details | binding site for residue SAO C 501 |
Chain | Residue |
C | GLN160 |
C | ARG169 |
C | GLY193 |
C | CYS194 |
C | GLU215 |
C | ALA216 |
C | GLY241 |
C | VAL243 |
C | GLU244 |
C | MET269 |
C | SER272 |
site_id | AC7 |
Number of Residues | 1 |
Details | binding site for residue EDO C 502 |
Chain | Residue |
C | PHE153 |
site_id | AC8 |
Number of Residues | 1 |
Details | binding site for residue DXE C 503 |
Chain | Residue |
C | TRP404 |
site_id | AC9 |
Number of Residues | 17 |
Details | binding site for residue 6D0 D 501 |
Chain | Residue |
D | PHE151 |
D | TYR154 |
D | GLN160 |
D | ARG169 |
D | GLY193 |
D | CYS194 |
D | SER196 |
D | ILE198 |
D | GLU215 |
D | ALA216 |
D | GLY241 |
D | LYS242 |
D | VAL243 |
D | GLU244 |
D | GLU258 |
D | MET269 |
D | SER272 |
site_id | AD1 |
Number of Residues | 2 |
Details | binding site for residue EDO D 502 |
Chain | Residue |
D | GLN149 |
D | PHE153 |
site_id | AD2 |
Number of Residues | 1 |
Details | binding site for residue DXE D 503 |
Chain | Residue |
D | TRP404 |
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 |