Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
| A | 0004523 | molecular_function | RNA-DNA hybrid ribonuclease activity |
| A | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
| B | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
| B | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1559 |
| Chain | Residue |
| A | ASP443 |
| A | GLU478 |
| A | ASP498 |
| A | MG1560 |
| A | MG1561 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1560 |
| Chain | Residue |
| A | MG1559 |
| A | HOH2235 |
| A | ASP443 |
| A | ASP498 |
| A | ASP549 |
| A | ARG557 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1561 |
| Chain | Residue |
| A | ASP443 |
| A | GLY444 |
| A | GLU478 |
| A | ARG557 |
| A | MG1559 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE TAR A 1562 |
| Chain | Residue |
| A | ARG211 |
| A | GLY436 |
| A | ALA437 |
| A | ASN460 |
| A | ARG461 |
| A | HOH2239 |
| B | ALA288 |
| B | THR290 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE WHU A 1563 |
| Chain | Residue |
| A | LEU100 |
| A | LYS101 |
| A | LYS102 |
| A | LYS103 |
| A | LYS104 |
| A | SER105 |
| A | VAL106 |
| A | VAL108 |
| A | VAL179 |
| A | TYR181 |
| A | LEU188 |
| A | PHE227 |
| A | TRP229 |
| A | LEU234 |
| A | HIS235 |
| A | PRO236 |
| A | TYR318 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 123 |
| Details | Domain: {"description":"RNase H type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00408","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Region: {"description":"RT 'primer grip'","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 32 |
| Details | Motif: {"description":"Tryptophan repeat motif","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12206668","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Site: {"description":"Cleavage; by viral protease","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Site: {"description":"Essential for RT p66/p51 heterodimerization","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Site: {"description":"Cleavage; by viral protease; partial","evidences":[{"evidenceCode":"ECO:0000250"}]} |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | |
| Details | M-CSA 175 |
