3REU
Crystal structure of the archaeal asparagine synthetase A complexed with L-Aspartic acid and Adenosine triphosphate
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 | 0006412 | biological_process | translation |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006421 | biological_process | asparaginyl-tRNA aminoacylation |
| A | 0046872 | molecular_function | metal ion binding |
| 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 | 0006412 | biological_process | translation |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006421 | biological_process | asparaginyl-tRNA aminoacylation |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 295 |
| Chain | Residue |
| A | GLU215 |
| A | SER218 |
| A | MG297 |
| A | ATP298 |
| A | HOH441 |
| A | HOH473 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 296 |
| Chain | Residue |
| A | HOH475 |
| A | HOH476 |
| A | ALA54 |
| A | ATP298 |
| A | HOH383 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 297 |
| Chain | Residue |
| A | ALA54 |
| A | GLU215 |
| A | MG295 |
| A | ATP298 |
| A | HOH441 |
| site_id | AC4 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ATP A 298 |
| Chain | Residue |
| A | ALA54 |
| A | ARG99 |
| A | GLU101 |
| A | ARG109 |
| A | HIS110 |
| A | SER111 |
| A | PHE114 |
| A | GLN116 |
| A | GLU215 |
| A | VAL216 |
| A | SER217 |
| A | GLY264 |
| A | ARG267 |
| A | MG295 |
| A | MG296 |
| A | MG297 |
| A | HOH305 |
| A | HOH309 |
| A | HOH383 |
| A | HOH464 |
| A | HOH473 |
| A | HOH477 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ASP B 295 |
| Chain | Residue |
| B | ASP47 |
| B | SER75 |
| B | LYS80 |
| B | ARG99 |
| B | GLN116 |
| B | ASP118 |
| B | SER218 |
| B | GLY219 |
| B | ARG222 |
| B | ALA261 |
| B | GLY262 |
| B | ATP299 |
| B | HOH355 |
| B | HOH378 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 296 |
| Chain | Residue |
| B | GLU215 |
| B | SER218 |
| B | MG297 |
| B | ATP299 |
| B | HOH354 |
| B | HOH371 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 297 |
| Chain | Residue |
| B | GLU215 |
| B | MG296 |
| B | ATP299 |
| B | HOH354 |
| B | HOH385 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 298 |
| Chain | Residue |
| B | ATP299 |
| B | HOH308 |
| B | HOH381 |
| B | HOH387 |
| B | HOH395 |
| site_id | AC9 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ATP B 299 |
| 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 | ASP295 |
| B | MG296 |
| B | MG297 |
| B | MG298 |
| B | HOH303 |
| B | HOH371 |
| B | HOH381 |
| B | HOH385 |
| B | HOH386 |
| B | HOH387 |
| B | HOH403 |
