3REX
Crystal structure of the archaeal asparagine synthetase A complexed with Adenosine monophosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004816 | molecular_function | asparagine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006421 | biological_process | asparaginyl-tRNA aminoacylation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004816 | molecular_function | asparagine-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006421 | biological_process | asparaginyl-tRNA aminoacylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE AMP A 295 |
| Chain | Residue |
| A | ARG99 |
| A | SER217 |
| A | SER218 |
| A | GLY264 |
| A | ARG267 |
| A | HOH312 |
| A | HOH324 |
| A | HOH388 |
| A | HOH392 |
| A | HOH394 |
| A | HOH446 |
| A | GLU101 |
| A | HOH452 |
| A | HOH463 |
| A | ARG109 |
| A | HIS110 |
| A | SER111 |
| A | PHE114 |
| A | GLN116 |
| A | GLU215 |
| A | VAL216 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 296 |
| Chain | Residue |
| A | ASP52 |
| A | HOH388 |
| A | HOH391 |
| A | HOH392 |
| A | HOH393 |
| A | HOH421 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE AMP B 295 |
| Chain | Residue |
| B | ARG99 |
| B | GLU101 |
| B | ARG109 |
| B | HIS110 |
| B | SER111 |
| B | PHE114 |
| B | GLN116 |
| B | GLU215 |
| B | VAL216 |
| B | SER217 |
| B | SER218 |
| B | GLY264 |
| B | ARG267 |
| B | HOH309 |
| B | HOH327 |
| B | HOH344 |
