4FNO
Crystal structure of peptidyl t-RNA hydrolase from Pseudomonas aeruginosa at 2.2 Angstrom resolution
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 | 7 |
| Details | BINDING SITE FOR RESIDUE PEG A 201 |
| Chain | Residue |
| A | LYS45 |
| A | PHE82 |
| B | ALA77 |
| B | ALA78 |
| B | GLY81 |
| B | PHE82 |
| B | PEG204 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 202 |
| Chain | Residue |
| A | GLY139 |
| A | TYR150 |
| A | GLU159 |
| A | HOH306 |
| A | HOH393 |
| A | HOH394 |
| A | PRO100 |
| A | PRO101 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 203 |
| Chain | Residue |
| A | GLU30 |
| A | LEU49 |
| A | ILE64 |
| A | HOH405 |
| B | ARG44 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 201 |
| Chain | Residue |
| B | GLY11 |
| B | ASN12 |
| B | PRO13 |
| B | ASN23 |
| B | ALA26 |
| B | ILE64 |
| B | PRO65 |
| B | THR66 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 202 |
| Chain | Residue |
| B | GLN5 |
| B | LYS58 |
| B | ASP59 |
| B | HOH345 |
| B | HOH383 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 203 |
| Chain | Residue |
| B | LEU97 |
| B | GLY113 |
| B | GLY114 |
| B | HIS140 |
| B | VAL147 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PEG B 204 |
| Chain | Residue |
| A | LYS45 |
| A | PHE47 |
| A | PEG201 |
| B | LYS45 |
| B | PHE47 |
| B | GLN74 |
| B | ALA78 |
Functional Information from PROSITE/UniProt
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"},{"source":"PubMed","id":"25101795","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00083","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"25101795","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| 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"},{"source":"PubMed","id":"25101795","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| 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"}]} |
| Chain | Residue | Details |
