1ASZ
THE ACTIVE SITE OF YEAST ASPARTYL-TRNA SYNTHETASE: STRUCTURAL AND FUNCTIONAL ASPECTS OF THE AMINOACYLATION REACTION
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 PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ATP A 701 |
| Chain | Residue |
| A | ARG325 |
| R | C675 |
| R | A676 |
| A | HIS334 |
| A | MET335 |
| A | PHE338 |
| A | GLU478 |
| A | ILE479 |
| A | LEU480 |
| A | GLY526 |
| A | ARG531 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ATP B 701 |
| Chain | Residue |
| B | ARG325 |
| B | MET335 |
| B | PHE338 |
| B | GLU478 |
| B | ILE479 |
| B | LEU480 |
| B | SER481 |
| B | ILE527 |
| B | ARG531 |
| S | C675 |
| S | A676 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | GLY282 | |
| B | HIS334 | |
| B | ILE479 | |
| B | GLY482 | |
| B | ILE486 | |
| B | LEU529 | |
| A | ALA326 | |
| A | HIS334 | |
| A | ILE479 | |
| A | GLY482 | |
| A | ILE486 | |
| A | LEU529 | |
| B | GLY282 | |
| B | ALA326 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | PRO302 | |
| B | PRO302 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | PRO503 | |
| B | PRO503 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358 |
| Chain | Residue | Details |
| A | LEU547 | |
| B | LEU547 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1asy |
| Chain | Residue | Details |
| A | ARG325 | |
| A | ARG531 | |
| A | ASP342 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1asy |
| Chain | Residue | Details |
| B | ARG325 | |
| B | ARG531 | |
| B | ASP342 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 404 |
| Chain | Residue | Details |
| A | ALA326 | electrostatic stabiliser |
| A | ASN328 | electrostatic stabiliser, metal ligand |
| A | HIS334 | electrostatic stabiliser, steric role |
| A | MET335 | electrostatic stabiliser, steric role |
| A | ILE479 | electrostatic stabiliser, metal ligand |
| A | GLY482 | electrostatic stabiliser, metal ligand |
| A | VAL532 | electrostatic stabiliser, steric role |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 404 |
| Chain | Residue | Details |
| B | ALA326 | electrostatic stabiliser |
| B | ASN328 | electrostatic stabiliser, metal ligand |
| B | HIS334 | electrostatic stabiliser, steric role |
| B | MET335 | electrostatic stabiliser, steric role |
| B | ILE479 | electrostatic stabiliser, metal ligand |
| B | GLY482 | electrostatic stabiliser, metal ligand |
| B | VAL532 | electrostatic stabiliser, steric role |
