2BE2
Crystal structure of HIV-1 reverse transcriptase (RT) in complex with R221239
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 SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
B | VAL111 | |
B | ASP186 | |
B | LEU187 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | SITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069 |
Chain | Residue | Details |
B | PRO1 | |
A | LEU479 | |
A | SER499 | |
A | LYS550 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Essential for RT p66/p51 heterodimerization |
Chain | Residue | Details |
B | TRP402 | |
B | GLU415 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | SITE: Essential for RT p66/p51 heterodimerization |
Chain | Residue | Details |
A | TRP402 | |
A | GLU415 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Cleavage; by viral protease; partial |
Chain | Residue | Details |
A | TYR441 |