8E14
Cryo-EM structure of Rous sarcoma virus strand transfer complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0015074 | biological_process | DNA integration |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0015074 | biological_process | DNA integration |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0008270 | molecular_function | zinc ion binding |
| C | 0015074 | biological_process | DNA integration |
| D | 0003676 | molecular_function | nucleic acid binding |
| D | 0008270 | molecular_function | zinc ion binding |
| D | 0015074 | biological_process | DNA integration |
| E | 0003676 | molecular_function | nucleic acid binding |
| E | 0008270 | molecular_function | zinc ion binding |
| E | 0015074 | biological_process | DNA integration |
| F | 0003676 | molecular_function | nucleic acid binding |
| F | 0008270 | molecular_function | zinc ion binding |
| F | 0015074 | biological_process | DNA integration |
| G | 0003676 | molecular_function | nucleic acid binding |
| G | 0008270 | molecular_function | zinc ion binding |
| G | 0015074 | biological_process | DNA integration |
| H | 0003676 | molecular_function | nucleic acid binding |
| H | 0008270 | molecular_function | zinc ion binding |
| H | 0015074 | biological_process | DNA integration |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 384 |
| Details | DNA_BIND: Integrase-type => ECO:0000255|PROSITE-ProRule:PRU00506 |
| Chain | Residue | Details |
| A | PRO222-THR270 | |
| B | PRO222-THR270 | |
| C | PRO222-THR270 | |
| D | PRO222-THR270 | |
| E | PRO222-THR270 | |
| F | PRO222-THR270 | |
| G | PRO222-THR270 | |
| H | PRO222-THR270 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00450 |
| Chain | Residue | Details |
| A | HIS9 | |
| E | HIS13 | |
| F | HIS9 | |
| F | HIS13 | |
| G | HIS9 | |
| G | HIS13 | |
| H | HIS9 | |
| H | HIS13 | |
| A | HIS13 | |
| B | HIS9 | |
| B | HIS13 | |
| C | HIS9 | |
| C | HIS13 | |
| D | HIS9 | |
| D | HIS13 | |
| E | HIS9 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00450, ECO:0000269|PubMed:26887497 |
| Chain | Residue | Details |
| A | CYS37 | |
| E | CYS40 | |
| F | CYS37 | |
| F | CYS40 | |
| G | CYS37 | |
| G | CYS40 | |
| H | CYS37 | |
| H | CYS40 | |
| A | CYS40 | |
| B | CYS37 | |
| B | CYS40 | |
| C | CYS37 | |
| C | CYS40 | |
| D | CYS37 | |
| D | CYS40 | |
| E | CYS37 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00405, ECO:0000269|PubMed:10669607 |
| Chain | Residue | Details |
| A | ASP64 | |
| E | ASP121 | |
| F | ASP64 | |
| F | ASP121 | |
| G | ASP64 | |
| G | ASP121 | |
| H | ASP64 | |
| H | ASP121 | |
| A | ASP121 | |
| B | ASP64 | |
| B | ASP121 | |
| C | ASP64 | |
| C | ASP121 | |
| D | ASP64 | |
| D | ASP121 | |
| E | ASP64 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:10669607 |
| Chain | Residue | Details |
| A | GLU157 | |
| B | GLU157 | |
| C | GLU157 | |
| D | GLU157 | |
| E | GLU157 | |
| F | GLU157 | |
| G | GLU157 | |
| H | GLU157 |
