2TS1
STRUCTURE OF TYROSYL-T/RNA SYNTHETASE REFINED AT 2.3 ANGSTROMS RESOLUTION. INTERACTION OF THE ENZYME WITH THE TYROSYL ADENYLATE INTERMEDIATE
Replaces: 1TS1Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004831 | molecular_function | tyrosine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006412 | biological_process | translation |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006437 | biological_process | tyrosyl-tRNA aminoacylation |
| A | 0016874 | molecular_function | ligase activity |
| A | 0032991 | cellular_component | protein-containing complex |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043039 | biological_process | tRNA aminoacylation |
| A | 0061635 | biological_process | regulation of protein complex stability |
Functional Information from PROSITE/UniProt
| site_id | PS00178 |
| Number of Residues | 11 |
| Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. Pt.ADsLHIGHL |
| Chain | Residue | Details |
| A | PRO39-LEU49 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 9 |
| Details | Motif: {"description":"'HIGH' region","evidences":[{"source":"PubMed","id":"11023794","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Motif: {"description":"'KMSKS' region","evidences":[{"source":"PubMed","id":"10630994","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1TYD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"},{"source":"PDB","id":"1TYD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 3284584 |
| Chain | Residue | Details |
| A | ARG86 | |
| A | LYS82 | |
| A | LYS233 | |
| A | LYS230 |
| site_id | MCSA1 |
| Number of Residues | 10 |
| Details | M-CSA 197 |
| Chain | Residue | Details |
| A | THR40 | electrostatic stabiliser, hydrogen bond donor |
| A | THR234 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, metal ligand |
| A | HIS45 | electrostatic stabiliser, hydrogen bond donor |
| A | HIS48 | electrostatic stabiliser, hydrogen bond donor |
| A | LYS82 | electrostatic stabiliser, hydrogen bond donor |
| A | ARG86 | electrostatic stabiliser, hydrogen bond donor |
| A | GLN173 | electrostatic stabiliser, hydrogen bond acceptor |
| A | ASP194 | electrostatic stabiliser, hydrogen bond acceptor |
| A | LYS230 | electrostatic stabiliser, hydrogen bond donor |
| A | LYS233 | electrostatic stabiliser, hydrogen bond donor |
