3LHD
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 | 0016426 | molecular_function | tRNA (adenine) methyltransferase activity |
| A | 0030488 | biological_process | tRNA methylation |
| A | 0031515 | cellular_component | tRNA (m1A) methyltransferase complex |
| A | 0043827 | molecular_function | tRNA (adenine(57)-N1)/(adenine(58)-N1)-methyltransferase activity |
| A | 0160107 | molecular_function | tRNA (adenine(58)-N1)-methyltransferase activity |
| B | 0016426 | molecular_function | tRNA (adenine) methyltransferase activity |
| B | 0030488 | biological_process | tRNA methylation |
| B | 0031515 | cellular_component | tRNA (m1A) methyltransferase complex |
| B | 0043827 | molecular_function | tRNA (adenine(57)-N1)/(adenine(58)-N1)-methyltransferase activity |
| B | 0160107 | molecular_function | tRNA (adenine(58)-N1)-methyltransferase activity |
| C | 0016426 | molecular_function | tRNA (adenine) methyltransferase activity |
| C | 0030488 | biological_process | tRNA methylation |
| C | 0031515 | cellular_component | tRNA (m1A) methyltransferase complex |
| C | 0043827 | molecular_function | tRNA (adenine(57)-N1)/(adenine(58)-N1)-methyltransferase activity |
| C | 0160107 | molecular_function | tRNA (adenine(58)-N1)-methyltransferase activity |
| D | 0016426 | molecular_function | tRNA (adenine) methyltransferase activity |
| D | 0030488 | biological_process | tRNA methylation |
| D | 0031515 | cellular_component | tRNA (m1A) methyltransferase complex |
| 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 | 11 |
| Details | BINDING SITE FOR RESIDUE SAH C 301 |
| Chain | Residue |
| C | GLY101 |
| C | PRO195 |
| C | HOH276 |
| C | GLY103 |
| C | GLU125 |
| C | ILE126 |
| C | PHE130 |
| C | LYS152 |
| C | ASP153 |
| C | ILE154 |
| C | TYR155 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE SAH A 301 |
| Chain | Residue |
| A | GLY101 |
| A | GLY103 |
| A | GLU125 |
| A | ILE126 |
| A | PHE130 |
| A | ASP153 |
| A | ILE154 |
| A | TYR155 |
| A | ASP169 |
| A | PRO171 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE SAH B 301 |
| Chain | Residue |
| B | GLY101 |
| B | GLY103 |
| B | GLU125 |
| B | ILE126 |
| B | PHE130 |
| B | LYS152 |
| B | ASP153 |
| B | ILE154 |
| B | TYR155 |
| B | ASP169 |
| B | LEU170 |
| B | HOH271 |
| B | HOH277 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE SAH D 301 |
| Chain | Residue |
| D | GLY101 |
| D | GLY103 |
| D | GLU125 |
| D | ILE126 |
| D | ARG127 |
| D | PHE130 |
| D | ASP153 |
| D | ILE154 |
| D | TYR155 |
| D | ASP169 |
| D | LEU170 |
| D | PRO171 |
| D | PRO195 |
| D | GLN199 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00952","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20483913","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
