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 | 11 |
| Details | BINDING SITE FOR RESIDUE M06 A 561 |
| Chain | Residue |
| A | LYS101 |
| A | PRO236 |
| A | TYR318 |
| A | ASN103 |
| A | VAL106 |
| A | TYR188 |
| A | PRO225 |
| A | PHE227 |
| A | TRP229 |
| A | LEU234 |
| A | HIS235 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| B | ASP110 | |
| B | ASP185 | |
| B | ASP186 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | SITE: Essential for RT p66/p51 heterodimerization => ECO:0000250 |
| Chain | Residue | Details |
| B | TRP401 | |
| B | TRP414 | |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | SITE: Cleavage; by viral protease; partial => ECO:0000250 |
| Chain | Residue | Details |
| B | PHE440 | |
| A | ASP549 | |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Essential for RT p66/p51 heterodimerization => ECO:0000250 |
| Chain | Residue | Details |
| A | TRP401 | |
| A | TRP414 | |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | SITE: Cleavage; by viral protease; partial => ECO:0000250 |
| Chain | Residue | Details |
| A | PHE440 | |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | SITE: Cleavage; by viral protease => ECO:0000250 |
| Chain | Residue | Details |
| A | LEU560 | |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | |
| Details | M-CSA 175 |
