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 |
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 | 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 | 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 |