4O2D
Crystal structure of aspartyl-tRNA synthetase from Mycobacterium smegmatis with bound aspartic acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004815 | molecular_function | aspartate-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006412 | biological_process | translation |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006422 | biological_process | aspartyl-tRNA aminoacylation |
| A | 0016874 | molecular_function | ligase activity |
| A | 0050560 | molecular_function | aspartate-tRNA(Asn) ligase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004815 | molecular_function | aspartate-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006412 | biological_process | translation |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006422 | biological_process | aspartyl-tRNA aminoacylation |
| B | 0016874 | molecular_function | ligase activity |
| B | 0050560 | molecular_function | aspartate-tRNA(Asn) ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE ASP A 801 |
| Chain | Residue |
| A | GLU171 |
| A | ARG490 |
| A | ILE532 |
| A | ALA533 |
| A | HOH934 |
| A | HOH979 |
| A | SER193 |
| A | GLN195 |
| A | LYS198 |
| A | ARG217 |
| A | GLN231 |
| A | HIS449 |
| A | HIS450 |
| A | GLY486 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE TRS A 802 |
| Chain | Residue |
| A | ASP282 |
| A | MET448 |
| A | HIS449 |
| A | ASP476 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE TRS A 803 |
| Chain | Residue |
| A | ASP31 |
| A | HIS32 |
| A | ASP520 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ASP B 801 |
| Chain | Residue |
| B | GLU171 |
| B | SER193 |
| B | GLN195 |
| B | LYS198 |
| B | ARG217 |
| B | GLN231 |
| B | HIS449 |
| B | HIS450 |
| B | GLY486 |
| B | ARG490 |
| B | ILE532 |
| B | ALA533 |
| B | HOH919 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE TRS B 802 |
| Chain | Residue |
| A | PRO109 |
| A | TYR124 |
| B | ARG28 |
| B | ARG30 |
| B | HIS32 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE TRS B 803 |
| Chain | Residue |
| A | GLN111 |
| B | ARG64 |
| B | ALA65 |
| B | HOH926 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00044 |
| Chain | Residue | Details |
| A | GLU171 | |
| B | GLN226 | |
| B | HIS449 | |
| B | GLU483 | |
| B | ARG490 | |
| B | GLY535 | |
| A | ARG217 | |
| A | GLN226 | |
| A | HIS449 | |
| A | GLU483 | |
| A | ARG490 | |
| A | GLY535 | |
| B | GLU171 | |
| B | ARG217 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | SITE: Important for tRNA non-discrimination => ECO:0000255|HAMAP-Rule:MF_00044 |
| Chain | Residue | Details |
| A | HIS32 | |
| A | GLY81 | |
| B | HIS32 | |
| B | GLY81 |
