5TBJ
Crystal structure of mouse CARM1 in complex with inhibitor LH1452
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 LHD A 501 |
Chain | Residue |
A | TYR150 |
A | VAL243 |
A | GLU244 |
A | GLU258 |
A | MET260 |
A | GLU267 |
A | MET269 |
A | SER272 |
A | HIS415 |
A | TRP416 |
A | EDO504 |
A | TYR154 |
A | HOH601 |
A | HOH627 |
A | HOH656 |
A | HOH689 |
A | GLN159 |
A | MET163 |
A | GLY193 |
A | GLU215 |
A | ALA216 |
A | GLY241 |
A | LYS242 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue PEG A 502 |
Chain | Residue |
A | LEU413 |
A | THR414 |
A | HIS415 |
A | TYR417 |
A | HOH684 |
site_id | AC3 |
Number of Residues | 1 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | LEU178 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue EDO A 504 |
Chain | Residue |
A | PHE153 |
A | GLU267 |
A | LHD501 |
site_id | AC5 |
Number of Residues | 1 |
Details | binding site for residue DXE A 505 |
Chain | Residue |
A | TRP404 |
site_id | AC6 |
Number of Residues | 25 |
Details | binding site for residue LHD B 501 |
Chain | Residue |
B | TYR150 |
B | PHE151 |
B | TYR154 |
B | GLN159 |
B | GLY193 |
B | GLU215 |
B | ALA216 |
B | GLY241 |
B | LYS242 |
B | VAL243 |
B | GLU244 |
B | GLU258 |
B | MET260 |
B | TYR262 |
B | GLU267 |
B | MET269 |
B | SER272 |
B | TRP416 |
B | HOH605 |
B | HOH606 |
B | HOH616 |
B | HOH623 |
B | HOH653 |
B | HOH678 |
B | HOH730 |
site_id | AC7 |
Number of Residues | 3 |
Details | binding site for residue EDO B 502 |
Chain | Residue |
A | ARG347 |
B | HOH666 |
B | HOH697 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue EDO B 503 |
Chain | Residue |
B | GLN149 |
B | TYR150 |
B | PHE153 |
B | HOH609 |
B | HOH715 |
site_id | AC9 |
Number of Residues | 2 |
Details | binding site for residue EDO B 504 |
Chain | Residue |
B | ASN359 |
B | GLU362 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue PG6 B 505 |
Chain | Residue |
A | LYS463 |
B | SER136 |
B | GLU244 |
B | GLU245 |
B | TYR279 |
site_id | AD2 |
Number of Residues | 4 |
Details | binding site for residue PEG B 506 |
Chain | Residue |
B | ASP458 |
B | THR460 |
B | GLY461 |
C | LEU178 |
site_id | AD3 |
Number of Residues | 1 |
Details | binding site for residue EDO B 507 |
Chain | Residue |
B | ASP393 |
site_id | AD4 |
Number of Residues | 22 |
Details | binding site for residue LHD C 501 |
Chain | Residue |
C | HOH675 |
C | TYR150 |
C | TYR154 |
C | GLN159 |
C | MET163 |
C | GLY193 |
C | GLU215 |
C | ALA216 |
C | GLY241 |
C | LYS242 |
C | VAL243 |
C | GLU244 |
C | GLU258 |
C | MET260 |
C | GLU267 |
C | MET269 |
C | SER272 |
C | HIS415 |
C | TRP416 |
C | HOH601 |
C | HOH650 |
C | HOH665 |
site_id | AD5 |
Number of Residues | 2 |
Details | binding site for residue PEG C 502 |
Chain | Residue |
C | HIS415 |
C | TYR417 |
site_id | AD6 |
Number of Residues | 1 |
Details | binding site for residue PEG C 503 |
Chain | Residue |
C | GLY398 |
site_id | AD7 |
Number of Residues | 2 |
Details | binding site for residue EDO C 504 |
Chain | Residue |
C | PHE153 |
C | HOH693 |
site_id | AD8 |
Number of Residues | 1 |
Details | binding site for residue EDO C 505 |
Chain | Residue |
C | TRP404 |
site_id | AD9 |
Number of Residues | 22 |
Details | binding site for residue LHD D 501 |
Chain | Residue |
D | TYR150 |
D | PHE151 |
D | TYR154 |
D | GLN159 |
D | MET163 |
D | GLY193 |
D | GLU215 |
D | ALA216 |
D | LYS242 |
D | VAL243 |
D | GLU244 |
D | GLU258 |
D | MET260 |
D | GLU267 |
D | MET269 |
D | SER272 |
D | HIS415 |
D | HOH618 |
D | HOH621 |
D | HOH632 |
D | HOH639 |
D | HOH715 |
site_id | AE1 |
Number of Residues | 1 |
Details | binding site for residue EDO D 502 |
Chain | Residue |
D | TYR150 |
site_id | AE2 |
Number of Residues | 1 |
Details | binding site for residue EDO D 503 |
Chain | Residue |
D | PHE475 |
site_id | AE3 |
Number of Residues | 2 |
Details | binding site for residue EDO D 504 |
Chain | Residue |
D | ASP393 |
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 |
D | GLY193 | |
D | GLU215 | |
D | GLU244 | |
D | SER272 | |
B | GLY193 | |
B | GLU215 | |
B | GLU244 | |
B | SER272 | |
C | GLN160 | |
C | ARG169 | |
C | GLY193 | |
C | GLU215 | |
C | GLU244 | |
C | SER272 | |
D | GLN160 | |
D | ARG169 | |
A | GLN160 | |
A | ARG169 | |
A | GLY193 | |
A | GLU215 | |
A | GLU244 | |
A | SER272 | |
B | GLN160 | |
B | ARG169 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:19843527 |
Chain | Residue | Details |
B | SER217 | |
C | SER217 | |
D | SER217 | |
A | 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 |