5DMQ
Crystal structure of mouse eRF1 in complex with Reverse Transcriptase (RT) of Moloney Murine Leukemia Virus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0004523 | molecular_function | RNA-DNA hybrid ribonuclease activity |
| B | 0000184 | biological_process | nuclear-transcribed mRNA catabolic process, nonsense-mediated decay |
| B | 0002184 | biological_process | cytoplasmic translational termination |
| B | 0003747 | molecular_function | translation release factor activity |
| B | 0004045 | molecular_function | peptidyl-tRNA hydrolase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006412 | biological_process | translation |
| B | 0006415 | biological_process | translational termination |
| B | 0006449 | biological_process | regulation of translational termination |
| B | 0006479 | biological_process | protein methylation |
| B | 0008079 | molecular_function | translation termination factor activity |
| B | 0016149 | molecular_function | translation release factor activity, codon specific |
| B | 0018444 | cellular_component | translation release factor complex |
| B | 0022626 | cellular_component | cytosolic ribosome |
| B | 0032790 | biological_process | ribosome disassembly |
| B | 1990825 | molecular_function | sequence-specific mRNA binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 21 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"A1Z651","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00405","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00408","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16912289","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00408","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"16912289","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Motif: {"description":"NIKS motif; plays an important role in translational termination","evidences":[{"source":"UniProtKB","id":"P62495","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"4-hydroxylysine","evidences":[{"source":"PubMed","id":"24486019","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N5-methylglutamine","evidences":[{"source":"PubMed","id":"20606008","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P62495","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P62495","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"P62495","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
