6ANQ
STRUCTURE OF HIV-1 REVERSE TRANSCRIPTASE (RT) TERNARY COMPLEX WITH A DOUBLE STRANDED DNA AND AN INCOMING D4TTP AT PH 8.5
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 |
| C | 0003676 | molecular_function | nucleic acid binding |
| C | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
| C | 0004523 | molecular_function | RNA-DNA hybrid ribonuclease activity |
| C | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
| D | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
| D | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | binding site for residue MG A 601 |
| Chain | Residue |
| A | ASP110 |
| A | VAL111 |
| A | ASP185 |
| A | D4T603 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 602 |
| Chain | Residue |
| A | ASP443 |
| A | GLU478 |
| A | ASP498 |
| A | HOH704 |
| T | HOH811 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | binding site for residue D4T A 603 |
| Chain | Residue |
| A | LYS65 |
| A | ARG72 |
| A | ASP110 |
| A | VAL111 |
| A | GLY112 |
| A | ASP113 |
| A | ALA114 |
| A | TYR115 |
| A | GLN151 |
| A | MET184 |
| A | ASP185 |
| A | LYS220 |
| A | MG601 |
| A | HOH729 |
| P | DDG822 |
| T | DA705 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 501 |
| Chain | Residue |
| A | LEU92 |
| A | VAL381 |
| B | GLN23 |
| B | PRO25 |
| B | PRO133 |
| B | ASN137 |
| B | HOH611 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| B | GLY316 |
| B | VAL317 |
| B | TYR318 |
| B | LYS323 |
| B | HOH602 |
| C | ASN418 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | GLU328 |
| B | TYR342 |
| B | PRO345 |
| B | PHE346 |
| B | ASN348 |
| B | TRP426 |
| B | HOH609 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| A | THR377 |
| A | ILE380 |
| B | PRO25 |
| B | THR400 |
| B | GOL505 |
| B | HOH665 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 505 |
| Chain | Residue |
| B | TRP24 |
| B | GLU399 |
| B | TRP402 |
| B | GOL504 |
| B | HOH625 |
| B | HOH655 |
| B | HOH665 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | binding site for residue GOL B 506 |
| Chain | Residue |
| A | TRP402 |
| A | HOH834 |
| B | LYS331 |
| B | GLY333 |
| B | GLN334 |
| B | GLY335 |
| B | GLN336 |
| B | TRP337 |
| B | HIS361 |
| B | ASP364 |
| B | GLN367 |
| site_id | AD1 |
| Number of Residues | 6 |
| Details | binding site for residue GOL B 507 |
| Chain | Residue |
| B | TYR232 |
| B | LEU234 |
| B | TRP239 |
| B | LYS374 |
| B | GLU378 |
| B | HOH629 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue MG C 601 |
| Chain | Residue |
| C | ASP110 |
| C | VAL111 |
| C | ASP185 |
| C | D4T603 |
| site_id | AD3 |
| Number of Residues | 6 |
| Details | binding site for residue MG C 602 |
| Chain | Residue |
| C | ASP443 |
| C | GLU478 |
| C | ASP498 |
| C | HOH713 |
| C | HOH741 |
| C | HOH785 |
| site_id | AD4 |
| Number of Residues | 14 |
| Details | binding site for residue D4T C 603 |
| Chain | Residue |
| C | LYS65 |
| C | ARG72 |
| C | ASP110 |
| C | VAL111 |
| C | GLY112 |
| C | ASP113 |
| C | ALA114 |
| C | TYR115 |
| C | GLN151 |
| C | MET184 |
| C | ASP185 |
| C | MG601 |
| E | DA705 |
| F | DDG822 |
| site_id | AD5 |
| Number of Residues | 7 |
| Details | binding site for residue GOL C 604 |
| Chain | Residue |
| C | THR403 |
| C | TYR405 |
| C | TRP406 |
| D | LYS331 |
| D | GLN332 |
| D | GLY333 |
| D | LYS424 |
| site_id | AD6 |
| Number of Residues | 6 |
| Details | binding site for residue GOL C 605 |
| Chain | Residue |
| C | TYR457 |
| C | ARG463 |
| C | GLN464 |
| C | LYS465 |
| C | ASP488 |
| C | HOH742 |
| site_id | AD7 |
| Number of Residues | 4 |
| Details | binding site for residue GOL D 501 |
| Chain | Residue |
| D | TYR342 |
| D | PHE346 |
| D | ASN348 |
| D | TRP426 |
| site_id | AD8 |
| Number of Residues | 8 |
| Details | binding site for residue GOL D 502 |
| Chain | Residue |
| C | LEU92 |
| C | VAL381 |
| D | GLN23 |
| D | TRP24 |
| D | PRO25 |
| D | PRO133 |
| D | ASN137 |
| D | HOH654 |
| site_id | AD9 |
| Number of Residues | 4 |
| Details | binding site for residue GOL D 503 |
| Chain | Residue |
| D | TRP24 |
| D | GLU399 |
| D | TRP402 |
| D | HOH673 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | ASP110 | |
| B | ASP185 | |
| B | ASP186 | |
| D | ASP110 | |
| D | ASP185 | |
| D | ASP186 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | SITE: Essential for RT p66/p51 heterodimerization |
| Chain | Residue | Details |
| B | TRP401 | |
| B | TRP414 | |
| D | TRP401 | |
| D | TRP414 | |
| C | ASP443 | |
| C | GLU478 | |
| C | ASP498 | |
| C | ASP549 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Essential for RT p66/p51 heterodimerization |
| Chain | Residue | Details |
| A | TRP401 | |
| A | TRP414 | |
| C | TRP401 | |
| C | TRP414 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by viral protease; partial |
| Chain | Residue | Details |
| A | PHE440 | |
| C | PHE440 |
