1ASY
CLASS II AMINOACYL TRANSFER RNA SYNTHETASES: CRYSTAL STRUCTURE OF YEAST ASPARTYL-TRNA SYNTHETASE COMPLEXED WITH TRNA ASP
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 | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006422 | biological_process | aspartyl-tRNA aminoacylation |
| 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 | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006422 | biological_process | aspartyl-tRNA aminoacylation |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Region: {"description":"Aspartate","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 2047877 |
| Chain | Residue | Details |
| B | ARG325 | |
| B | ARG531 | |
| B | ASP342 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 2047877 |
| Chain | Residue | Details |
| A | ARG325 | |
| A | ARG531 | |
| A | ASP342 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 404 |
| Chain | Residue | Details |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 404 |
| Chain | Residue | Details |
