5ISH
Crystal structure of mouse CARM1 in complex with inhibitor SA0765
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 765 A 501 |
Chain | Residue |
A | TYR150 |
A | LEU199 |
A | GLU215 |
A | ALA216 |
A | GLY241 |
A | LYS242 |
A | VAL243 |
A | GLU244 |
A | GLU258 |
A | MET269 |
A | SER272 |
A | PHE151 |
A | HOH639 |
A | HOH655 |
A | HOH656 |
A | HOH707 |
A | TYR154 |
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 | GLU411 |
A | HOH668 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue PEG A 503 |
Chain | Residue |
A | PHE153 |
A | GLU267 |
A | HOH671 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue PEG A 505 |
Chain | Residue |
A | LEU178 |
A | GLN205 |
A | HOH603 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue DXE A 506 |
Chain | Residue |
A | TRP404 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue M2M A 507 |
Chain | Residue |
A | TYR304 |
A | PRO317 |
A | VAL332 |
A | ASP333 |
A | GLN424 |
A | SER425 |
site_id | AC7 |
Number of Residues | 22 |
Details | binding site for residue 765 B 501 |
Chain | Residue |
B | TYR150 |
B | PHE151 |
B | TYR154 |
B | MET163 |
B | ARG169 |
B | GLY193 |
B | CYS194 |
B | ILE198 |
B | LEU199 |
B | GLU215 |
B | ALA216 |
B | GLY241 |
B | LYS242 |
B | VAL243 |
B | GLU244 |
B | MET269 |
B | SER272 |
B | HOH612 |
B | HOH624 |
B | HOH673 |
B | HOH678 |
B | HOH714 |
site_id | AC8 |
Number of Residues | 1 |
Details | binding site for residue EDO B 502 |
Chain | Residue |
B | TRP404 |
site_id | AC9 |
Number of Residues | 4 |
Details | binding site for residue PEG B 504 |
Chain | Residue |
B | ASN162 |
B | ASP166 |
B | LEU413 |
B | HIS415 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue PG4 B 505 |
Chain | Residue |
A | LYS463 |
B | SER136 |
B | GLU244 |
B | GLU245 |
B | HOH739 |
site_id | AD2 |
Number of Residues | 22 |
Details | binding site for residue 765 C 501 |
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 | HOH623 |
C | HOH627 |
C | HOH674 |
C | HOH706 |
site_id | AD3 |
Number of Residues | 2 |
Details | binding site for residue EDO C 502 |
Chain | Residue |
C | GLN149 |
C | PHE153 |
site_id | AD4 |
Number of Residues | 1 |
Details | binding site for residue EDO C 503 |
Chain | Residue |
C | GLY398 |
site_id | AD5 |
Number of Residues | 3 |
Details | binding site for residue EDO C 504 |
Chain | Residue |
C | THR410 |
C | GLU411 |
C | HOH758 |
site_id | AD6 |
Number of Residues | 2 |
Details | binding site for residue EDO C 505 |
Chain | Residue |
C | SER399 |
C | LYS187 |
site_id | AD7 |
Number of Residues | 1 |
Details | binding site for residue DXE C 506 |
Chain | Residue |
C | TRP404 |
site_id | AD8 |
Number of Residues | 5 |
Details | binding site for residue DXE C 507 |
Chain | Residue |
C | VAL332 |
C | ASP333 |
C | GLN424 |
C | SER425 |
C | HOH686 |
site_id | AD9 |
Number of Residues | 3 |
Details | binding site for residue DXE C 508 |
Chain | Residue |
C | LYS277 |
C | LEU361 |
C | HOH756 |
site_id | AE1 |
Number of Residues | 2 |
Details | binding site for residue DXE C 509 |
Chain | Residue |
C | LEU178 |
C | GLN205 |
site_id | AE2 |
Number of Residues | 23 |
Details | binding site for residue 765 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 | MET269 |
D | SER272 |
D | HOH607 |
D | HOH619 |
D | HOH631 |
D | HOH715 |
site_id | AE3 |
Number of Residues | 1 |
Details | binding site for residue EDO D 502 |
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 |