Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000049 | molecular_function | tRNA binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004045 | molecular_function | peptidyl-tRNA hydrolase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006515 | biological_process | protein quality control for misfolded or incompletely synthesized proteins |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0072344 | biological_process | rescue of stalled ribosome |
| B | 0000049 | molecular_function | tRNA binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004045 | molecular_function | peptidyl-tRNA hydrolase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006515 | biological_process | protein quality control for misfolded or incompletely synthesized proteins |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0072344 | biological_process | rescue of stalled ribosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 201 |
| Chain | Residue |
| A | ARG50 |
| A | LYS55 |
| B | TYR79 |
| B | HOH309 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 202 |
| Chain | Residue |
| A | ARG50 |
| B | TYR78 |
| B | TYR79 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 203 |
| Chain | Residue |
| A | ASP153 |
| A | HOH330 |
| A | SER151 |
| A | ASN152 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue GOL A 204 |
| Chain | Residue |
| A | ARG103 |
| A | GLN104 |
| A | MET182 |
| A | HOH329 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 201 |
| Chain | Residue |
| A | ARG177 |
| B | GLN104 |
| B | SER176 |
| B | ARG177 |
| B | PHE178 |
| B | ASP179 |
Functional Information from PROSITE/UniProt
| site_id | PS01195 |
| Number of Residues | 14 |
| Details | PEPT_TRNA_HYDROL_1 Peptidyl-tRNA hydrolase signature 1. FelTRHNiGfeVVD |
| Chain | Residue | Details |
| A | PHE14-ASP27 | |
| site_id | PS01196 |
| Number of Residues | 11 |
| Details | PEPT_TRNA_HYDROL_2 Peptidyl-tRNA hydrolase signature 2. SaggHNGMKSI |
| Chain | Residue | Details |
| A | SER107-ILE117 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Discriminates between blocked and unblocked aminoacyl-tRNA","evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Site: {"description":"Stabilizes the basic form of H active site to accept a proton","evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"}]} |
