4TS1
CRYSTAL STRUCTURE OF A DELETION MUTANT OF A TYROSYL-T/RNA SYNTHETASE COMPLEXED WITH TYROSINE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004831 | molecular_function | tyrosine-tRNA ligase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| A | 0006437 | biological_process | tyrosyl-tRNA aminoacylation |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004831 | molecular_function | tyrosine-tRNA ligase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| B | 0006437 | biological_process | tyrosyl-tRNA aminoacylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE TYR A 320 |
| Chain | Residue |
| A | TYR34 |
| A | GLN195 |
| A | HOH348 |
| A | HOH375 |
| A | GLY36 |
| A | ASP38 |
| A | LEU68 |
| A | ASP78 |
| A | TYR169 |
| A | GLN173 |
| A | ASP176 |
| A | GLN189 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE TYR B 320 |
| Chain | Residue |
| B | TYR34 |
| B | GLY36 |
| B | ASP38 |
| B | ASP78 |
| B | TYR169 |
| B | GLN173 |
| B | ASP176 |
| B | GLN189 |
| B | GLN195 |
| B | HOH351 |
| B | HOH389 |
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 | 18 |
| Details | Motif: {"description":"'HIGH' region","evidences":[{"source":"PubMed","id":"11023794","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Motif: {"description":"'KMSKS' region","evidences":[{"source":"PubMed","id":"10630994","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1TYD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| 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 | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1d2r |
| Chain | Residue | Details |
| A | LYS233 | |
| A | LYS230 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1d2r |
| Chain | Residue | Details |
| B | LYS233 | |
| B | LYS230 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1d2r |
| Chain | Residue | Details |
| A | ARG86 | |
| A | LYS82 | |
| A | LYS233 | |
| A | LYS230 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1d2r |
| Chain | Residue | Details |
| B | ARG86 | |
| B | LYS82 | |
| B | LYS233 | |
| B | 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 |
| site_id | MCSA2 |
| Number of Residues | 10 |
| Details | M-CSA 197 |
| Chain | Residue | Details |
| B | THR40 | electrostatic stabiliser, hydrogen bond donor |
| B | THR234 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, metal ligand |
| B | HIS45 | electrostatic stabiliser, hydrogen bond donor |
| B | HIS48 | electrostatic stabiliser, hydrogen bond donor |
| B | LYS82 | electrostatic stabiliser, hydrogen bond donor |
| B | ARG86 | electrostatic stabiliser, hydrogen bond donor |
| B | GLN173 | electrostatic stabiliser, hydrogen bond acceptor |
| B | ASP194 | electrostatic stabiliser, hydrogen bond acceptor |
| B | LYS230 | electrostatic stabiliser, hydrogen bond donor |
| B | LYS233 | electrostatic stabiliser, hydrogen bond donor |
