4NBI
D-aminoacyl-tRNA deacylase (DTD) from Plasmodium falciparum in complex with D-tyrosyl-3'-aminoadenosine at 1.86 Angstrom resolution
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0002161 | molecular_function | aminoacyl-tRNA editing activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006399 | biological_process | tRNA metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0051499 | molecular_function | D-aminoacyl-tRNA deacylase activity |
| A | 0051500 | molecular_function | D-tyrosyl-tRNA(Tyr) deacylase activity |
| A | 0106026 | molecular_function | Gly-tRNA(Ala) hydrolase activity |
| A | 0106074 | biological_process | aminoacyl-tRNA metabolism involved in translational fidelity |
| B | 0000049 | molecular_function | tRNA binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0002161 | molecular_function | aminoacyl-tRNA editing activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006399 | biological_process | tRNA metabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0051499 | molecular_function | D-aminoacyl-tRNA deacylase activity |
| B | 0051500 | molecular_function | D-tyrosyl-tRNA(Tyr) deacylase activity |
| B | 0106026 | molecular_function | Gly-tRNA(Ala) hydrolase activity |
| B | 0106074 | biological_process | aminoacyl-tRNA metabolism involved in translational fidelity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE D3Y A 201 |
| Chain | Residue |
| A | LEU41 |
| A | ASN139 |
| A | HOH648 |
| A | HOH705 |
| B | GLY149 |
| B | PRO150 |
| A | ILE43 |
| A | SER87 |
| A | GLN88 |
| A | PHE89 |
| A | LYS107 |
| A | ALA112 |
| A | PHE137 |
| A | GLY138 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PGE A 502 |
| Chain | Residue |
| A | ASP144 |
| A | THR146 |
| B | GLY10 |
| B | ILE12 |
| B | THR146 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE D3Y B 201 |
| Chain | Residue |
| A | GLY149 |
| A | PRO150 |
| B | LEU41 |
| B | ILE43 |
| B | SER87 |
| B | GLN88 |
| B | PHE89 |
| B | LYS107 |
| B | PHE137 |
| B | GLY138 |
| B | ASN139 |
| B | HOH343 |
| B | HOH345 |
| B | HOH368 |
| B | HOH393 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:20007323 |
| Chain | Residue | Details |
| A | THR90 | |
| B | THR90 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:20007323, ECO:0007744|PDB:3KO5 |
| Chain | Residue | Details |
| A | TRP72 | |
| B | TRP72 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:20007323, ECO:0007744|PDB:3KO4, ECO:0007744|PDB:3KO5 |
| Chain | Residue | Details |
| A | PHE89 | |
| B | PHE89 |
