6CU3
Crystal structure of a protein arginine N-methyltransferase from Naegleria fowleri
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005634 | cellular_component | nucleus |
| A | 0006338 | biological_process | chromatin remodeling |
| A | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
| A | 0018216 | biological_process | peptidyl-arginine methylation |
| A | 0035242 | molecular_function | protein-arginine omega-N asymmetric methyltransferase activity |
| A | 0042054 | molecular_function | histone methyltransferase activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0006338 | biological_process | chromatin remodeling |
| B | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
| B | 0018216 | biological_process | peptidyl-arginine methylation |
| B | 0035242 | molecular_function | protein-arginine omega-N asymmetric methyltransferase activity |
| B | 0042054 | molecular_function | histone methyltransferase activity |
| C | 0005634 | cellular_component | nucleus |
| C | 0006338 | biological_process | chromatin remodeling |
| C | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
| C | 0018216 | biological_process | peptidyl-arginine methylation |
| C | 0035242 | molecular_function | protein-arginine omega-N asymmetric methyltransferase activity |
| C | 0042054 | molecular_function | histone methyltransferase activity |
| D | 0005634 | cellular_component | nucleus |
| D | 0006338 | biological_process | chromatin remodeling |
| D | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
| D | 0018216 | biological_process | peptidyl-arginine methylation |
| D | 0035242 | molecular_function | protein-arginine omega-N asymmetric methyltransferase activity |
| D | 0042054 | molecular_function | histone methyltransferase activity |
| E | 0005634 | cellular_component | nucleus |
| E | 0006338 | biological_process | chromatin remodeling |
| E | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
| E | 0018216 | biological_process | peptidyl-arginine methylation |
| E | 0035242 | molecular_function | protein-arginine omega-N asymmetric methyltransferase activity |
| E | 0042054 | molecular_function | histone methyltransferase activity |
| F | 0005634 | cellular_component | nucleus |
| F | 0006338 | biological_process | chromatin remodeling |
| F | 0016274 | molecular_function | protein-arginine N-methyltransferase activity |
| F | 0018216 | biological_process | peptidyl-arginine methylation |
| F | 0035242 | molecular_function | protein-arginine omega-N asymmetric methyltransferase activity |
| F | 0042054 | molecular_function | histone methyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 2 |
| Details | binding site for residue EDO A 401 |
| Chain | Residue |
| A | ARG82 |
| A | LYS98 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | LYS45 |
| A | ASP115 |
| A | PRO145 |
| E | ASP44 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | THR155 |
| A | LYS209 |
| A | GLU212 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | ASP163 |
| A | TYR166 |
| A | ASP196 |
| A | GLN202 |
| A | TYR278 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | THR206 |
| A | GLN235 |
| A | ASN288 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | binding site for residue EDO B 401 |
| Chain | Residue |
| B | LEU22 |
| B | LYS23 |
| B | ASP24 |
| B | ARG27 |
| B | THR28 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| B | ARG82 |
| B | LYS98 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | ASP44 |
| B | LYS45 |
| B | ASP115 |
| B | ARG144 |
| B | PRO145 |
| B | TYR148 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | binding site for residue EDO B 404 |
| Chain | Residue |
| B | GLY123 |
| B | TYR124 |
| B | HIS271 |
| B | TRP272 |
| site_id | AD1 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 405 |
| Chain | Residue |
| B | LEU223 |
| B | ILE226 |
| B | GLN299 |
| site_id | AD2 |
| Number of Residues | 3 |
| Details | binding site for residue EDO C 401 |
| Chain | Residue |
| C | TYR239 |
| E | GLN237 |
| E | TYR239 |
| site_id | AD3 |
| Number of Residues | 2 |
| Details | binding site for residue EDO E 401 |
| Chain | Residue |
| E | ARG82 |
| E | LYS98 |
| site_id | AD4 |
| Number of Residues | 4 |
| Details | binding site for residue EDO E 402 |
| Chain | Residue |
| E | MET122 |
| E | TYR124 |
| E | HIS271 |
| E | TRP272 |
| site_id | AD5 |
| Number of Residues | 3 |
| Details | binding site for residue EDO E 403 |
| Chain | Residue |
| E | ASP175 |
| E | ASN176 |
| E | GLY179 |
| site_id | AD6 |
| Number of Residues | 3 |
| Details | binding site for residue EDO E 404 |
| Chain | Residue |
| E | GLU192 |
| E | ARG328 |
| E | EDO405 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue EDO E 405 |
| Chain | Residue |
| E | TYR124 |
| E | VAL195 |
| E | LYS273 |
| E | EDO404 |
| site_id | AD8 |
| Number of Residues | 2 |
| Details | binding site for residue EDO E 406 |
| Chain | Residue |
| E | LEU223 |
| E | GLN299 |
| site_id | AD9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO E 407 |
| Chain | Residue |
| E | LEU283 |
| E | PRO284 |
| E | VAL315 |
