3LGA
Crystal structure of P. abyssi tRNA m1A58 methyltransferase in complex with S-adenosyl-L-homocysteine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008033 | biological_process | tRNA processing |
| A | 0008168 | molecular_function | methyltransferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030488 | biological_process | tRNA methylation |
| A | 0031515 | cellular_component | tRNA (m1A) methyltransferase complex |
| A | 0032259 | biological_process | methylation |
| A | 0043827 | molecular_function | tRNA (adenine(57)-N1)/(adenine(58)-N1)-methyltransferase activity |
| A | 0160107 | molecular_function | tRNA (adenine(58)-N1)-methyltransferase activity |
| B | 0008033 | biological_process | tRNA processing |
| B | 0008168 | molecular_function | methyltransferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030488 | biological_process | tRNA methylation |
| B | 0031515 | cellular_component | tRNA (m1A) methyltransferase complex |
| B | 0032259 | biological_process | methylation |
| B | 0043827 | molecular_function | tRNA (adenine(57)-N1)/(adenine(58)-N1)-methyltransferase activity |
| B | 0160107 | molecular_function | tRNA (adenine(58)-N1)-methyltransferase activity |
| C | 0008033 | biological_process | tRNA processing |
| C | 0008168 | molecular_function | methyltransferase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0030488 | biological_process | tRNA methylation |
| C | 0031515 | cellular_component | tRNA (m1A) methyltransferase complex |
| C | 0032259 | biological_process | methylation |
| C | 0043827 | molecular_function | tRNA (adenine(57)-N1)/(adenine(58)-N1)-methyltransferase activity |
| C | 0160107 | molecular_function | tRNA (adenine(58)-N1)-methyltransferase activity |
| D | 0008033 | biological_process | tRNA processing |
| D | 0008168 | molecular_function | methyltransferase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0030488 | biological_process | tRNA methylation |
| D | 0031515 | cellular_component | tRNA (m1A) methyltransferase complex |
| D | 0032259 | biological_process | methylation |
| D | 0043827 | molecular_function | tRNA (adenine(57)-N1)/(adenine(58)-N1)-methyltransferase activity |
| D | 0160107 | molecular_function | tRNA (adenine(58)-N1)-methyltransferase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE SAH A 301 |
| Chain | Residue |
| A | GLN75 |
| A | LEU107 |
| A | GLU125 |
| A | ILE126 |
| A | ARG127 |
| A | PHE130 |
| A | ASP153 |
| A | ILE154 |
| A | TYR155 |
| A | ASP169 |
| A | LEU170 |
| A | ILE76 |
| A | PRO171 |
| A | HOH282 |
| A | HOH323 |
| A | HOH328 |
| A | VAL77 |
| A | GLY101 |
| A | VAL102 |
| A | GLY103 |
| A | SER104 |
| A | GLY105 |
| A | ALA106 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SAH B 301 |
| Chain | Residue |
| B | GLN75 |
| B | ILE76 |
| B | VAL77 |
| B | GLY101 |
| B | VAL102 |
| B | GLY103 |
| B | SER104 |
| B | GLY105 |
| B | ALA106 |
| B | LEU107 |
| B | GLU125 |
| B | ILE126 |
| B | ARG127 |
| B | PHE130 |
| B | ASP153 |
| B | ILE154 |
| B | TYR155 |
| B | ASP169 |
| B | LEU170 |
| B | PRO171 |
| B | HOH267 |
| B | HOH318 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE SAH C 301 |
| Chain | Residue |
| C | GLN75 |
| C | ILE76 |
| C | VAL77 |
| C | GLY101 |
| C | VAL102 |
| C | GLY103 |
| C | SER104 |
| C | GLY105 |
| C | ALA106 |
| C | LEU107 |
| C | GLU125 |
| C | ILE126 |
| C | ARG127 |
| C | PHE130 |
| C | ASP153 |
| C | ILE154 |
| C | TYR155 |
| C | ASP169 |
| C | LEU170 |
| C | PRO171 |
| C | HOH275 |
| C | HOH311 |
| C | HOH336 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE SAH D 301 |
| Chain | Residue |
| D | GLN75 |
| D | VAL77 |
| D | GLY101 |
| D | VAL102 |
| D | GLY103 |
| D | SER104 |
| D | GLY105 |
| D | ALA106 |
| D | LEU107 |
| D | GLU125 |
| D | ILE126 |
| D | ARG127 |
| D | PHE130 |
| D | ASP153 |
| D | ILE154 |
| D | TYR155 |
| D | ASP169 |
| D | LEU170 |
| D | PRO171 |
| D | HOH288 |
| D | HOH312 |
| D | HOH331 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 D 254 |
| Chain | Residue |
| D | LYS16 |
| D | ARG17 |
| D | LYS69 |
| D | HOH255 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 254 |
| Chain | Residue |
| A | LYS16 |
| A | ARG17 |
| A | LYS69 |
| A | HOH255 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 254 |
| Chain | Residue |
| B | LYS69 |
| B | HOH255 |
| B | ARG17 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 254 |
| Chain | Residue |
| C | LYS16 |
| C | ARG17 |
| C | LYS69 |
| C | HOH256 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | SER104 | |
| B | SER104 | |
| C | SER104 | |
| D | SER104 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00952, ECO:0000269|PubMed:20483913 |
| Chain | Residue | Details |
| A | GLU125 | |
| D | GLU125 | |
| D | ASP153 | |
| D | ASP169 | |
| A | ASP153 | |
| A | ASP169 | |
| B | GLU125 | |
| B | ASP153 | |
| B | ASP169 | |
| C | GLU125 | |
| C | ASP153 | |
| C | ASP169 |
