7SJX
Cryo-EM Structure of the PR-RT components of the HIV-1 Pol Polyprotein
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003677 | molecular_function | DNA binding |
| A | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
| A | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| A | 0004521 | molecular_function | RNA endonuclease activity |
| A | 0004523 | molecular_function | RNA-DNA hybrid ribonuclease activity |
| A | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
| A | 0006508 | biological_process | proteolysis |
| A | 0008270 | molecular_function | zinc ion binding |
| A | 0015074 | biological_process | DNA integration |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0003677 | molecular_function | DNA binding |
| B | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
| B | 0004190 | molecular_function | aspartic-type endopeptidase activity |
| B | 0004521 | molecular_function | RNA endonuclease activity |
| B | 0004523 | molecular_function | RNA-DNA hybrid ribonuclease activity |
| B | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
| B | 0006508 | biological_process | proteolysis |
| B | 0008270 | molecular_function | zinc ion binding |
| B | 0015074 | biological_process | DNA integration |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 138 |
| Details | Domain: {"description":"Peptidase A2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00275","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 44 |
| Details | Region: {"description":"Dimerization of protease","evidences":[{"source":"UniProtKB","id":"P04585","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Region: {"description":"RT 'primer grip'"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 32 |
| Details | Motif: {"description":"Tryptophan repeat motif"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Active site: {"description":"For protease activity; shared with dimeric partner","evidences":[{"source":"PROSITE-ProRule","id":"PRU10094","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12924029","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Site: {"description":"Cleavage; by viral protease","evidences":[{"source":"PubMed","id":"2476069","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Site: {"description":"Essential for RT p66/p51 heterodimerization"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Site: {"description":"Cleavage; by viral protease; partial"} |
| Chain | Residue | Details |
