1YID
Crystal structure of tryptophanyl tRNA synthetase II from Deinococcus radiodurans in complex with ATP.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| A | 0004830 | molecular_function | tryptophan-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 | 0006436 | biological_process | tryptophanyl-tRNA aminoacylation |
| A | 0016874 | molecular_function | ligase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| B | 0004830 | molecular_function | tryptophan-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 | 0006436 | biological_process | tryptophanyl-tRNA aminoacylation |
| B | 0016874 | molecular_function | ligase activity |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
| C | 0004830 | molecular_function | tryptophan-tRNA ligase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006412 | biological_process | translation |
| C | 0006418 | biological_process | tRNA aminoacylation for protein translation |
| C | 0006436 | biological_process | tryptophanyl-tRNA aminoacylation |
| C | 0016874 | molecular_function | ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG B 3001 |
| Chain | Residue |
| B | ATP3000 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ATP B 3000 |
| Chain | Residue |
| B | SER217 |
| B | SER219 |
| B | MG3001 |
| B | GLY28 |
| B | ASP29 |
| B | ARG30 |
| B | GLY38 |
| B | HIS39 |
| B | ARG206 |
| B | LEU207 |
| B | MET216 |
Functional Information from PROSITE/UniProt
| site_id | PS00178 |
| Number of Residues | 10 |
| Details | AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. P..TGaLHLGHL |
| Chain | Residue | Details |
| B | PRO31-LEU40 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Motif: {"description":"'HIGH' region"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Motif: {"description":"'KMSKS' region"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| 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 |
| B | LYS215 | |
| B | LYS218 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1d2r |
| Chain | Residue | Details |
| A | LYS215 | |
| A | LYS218 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1d2r |
| Chain | Residue | Details |
| C | LYS215 | |
| C | LYS218 |
