4LWP
Crystal structure of PRMT6-SAH
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005634 | cellular_component | nucleus |
A | 0005829 | cellular_component | cytosol |
A | 0006338 | biological_process | chromatin remodeling |
A | 0008168 | molecular_function | methyltransferase activity |
A | 0008469 | molecular_function | histone arginine N-methyltransferase activity |
A | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0018216 | biological_process | peptidyl-arginine methylation |
A | 0019919 | biological_process | peptidyl-arginine methylation, to asymmetrical-dimethyl arginine |
A | 0032259 | biological_process | methylation |
A | 0034969 | biological_process | obsolete histone arginine methylation |
A | 0035244 | molecular_function | protein-arginine C-methyltransferase activity |
B | 0005634 | cellular_component | nucleus |
B | 0005829 | cellular_component | cytosol |
B | 0006338 | biological_process | chromatin remodeling |
B | 0008168 | molecular_function | methyltransferase activity |
B | 0008469 | molecular_function | histone arginine N-methyltransferase activity |
B | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
B | 0016740 | molecular_function | transferase activity |
B | 0018216 | biological_process | peptidyl-arginine methylation |
B | 0019919 | biological_process | peptidyl-arginine methylation, to asymmetrical-dimethyl arginine |
B | 0032259 | biological_process | methylation |
B | 0034969 | biological_process | obsolete histone arginine methylation |
B | 0035244 | molecular_function | protein-arginine C-methyltransferase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD B 401 |
Chain | Residue |
B | THR185 |
B | SER302 |
site_id | AC2 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD B 402 |
Chain | Residue |
B | ASN251 |
site_id | AC3 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD B 404 |
Chain | Residue |
B | ARG126 |
B | HIS127 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD B 405 |
Chain | Residue |
B | HIS318 |
site_id | AC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE SAH B 407 |
Chain | Residue |
B | SER63 |
B | GLY64 |
B | ILE67 |
B | GLU84 |
B | ALA85 |
B | ASP110 |
B | THR111 |
B | VAL112 |
B | GLU113 |
B | GLU142 |
B | MET153 |
B | SER156 |
B | HOH503 |
B | HOH507 |
B | HIS30 |
B | ARG39 |
B | GLY62 |
site_id | AC6 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE SAH A 401 |
Chain | Residue |
A | HIS30 |
A | MET33 |
A | ARG39 |
A | GLY62 |
A | SER63 |
A | GLY64 |
A | GLU84 |
A | ALA85 |
A | ASP110 |
A | THR111 |
A | VAL112 |
A | GLU113 |
A | GLU142 |
A | MET153 |
A | SER156 |
A | HOH502 |
A | HOH504 |
site_id | AC7 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE IOD A 402 |
Chain | Residue |
A | THR185 |
A | SER302 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD A 403 |
Chain | Residue |
B | HIS268 |
site_id | AC9 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE IOD A 404 |
Chain | Residue |
A | HIS127 |
site_id | BC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PGE A 405 |
Chain | Residue |
A | PRO195 |
A | GLN199 |
A | LEU238 |
A | GLU283 |