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 | 14 |
Details | BINDING SITE FOR RESIDUE T27 A 601 |
Chain | Residue |
A | LEU100 |
A | PRO236 |
A | TYR318 |
A | HOH925 |
B | GLU138 |
B | HOH632 |
A | LYS101 |
A | LYS103 |
A | TYR181 |
A | TYR188 |
A | PHE227 |
A | TRP229 |
A | LEU234 |
A | HIS235 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMQ A 602 |
Chain | Residue |
A | LEU469 |
A | GLN480 |
A | LEU484 |
A | GLU516 |
A | LEU517 |
A | GLN520 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE DMS A 603 |
Chain | Residue |
A | TRP401 |
A | LEU425 |
A | TRP426 |
A | TYR427 |
A | GLN509 |
A | ASP511 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMS A 604 |
Chain | Residue |
A | GLN428 |
A | LEU525 |
A | LYS528 |
A | GLU529 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS A 605 |
Chain | Residue |
A | LYS331 |
A | GLY333 |
A | GLN334 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMS A 606 |
Chain | Residue |
A | THR473 |
A | ASN474 |
A | GLN475 |
A | HOH1012 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 607 |
Chain | Residue |
A | ASP443 |
A | ASP498 |
A | ASP549 |
A | HOH866 |
A | HOH967 |
A | HOH1031 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE FMQ B 501 |
Chain | Residue |
A | THR377 |
A | ILE380 |
B | TRP24 |
B | PRO25 |
B | GLU399 |
B | THR400 |
B | TRP402 |
B | DMS502 |
B | HOH628 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE DMS B 502 |
Chain | Residue |
B | THR27 |
B | THR400 |
B | TRP401 |
B | GLU404 |
B | FMQ501 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS B 503 |
Chain | Residue |
A | GLN85 |
B | TYR56 |
B | LYS126 |
site_id | BC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE DMS B 504 |
Chain | Residue |
A | ILE380 |
A | VAL381 |
B | PRO25 |
B | LEU26 |
B | PRO133 |
B | SER134 |
B | ILE135 |
B | HOH810 |
site_id | BC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE DMS B 505 |
Chain | Residue |
B | LEU234 |
B | HIS235 |
B | TRP239 |
site_id | BC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMS B 506 |
Chain | Residue |
A | GLU138 |
B | GLN269 |
B | LEU422 |
B | TRP426 |
site_id | BC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE DMS B 507 |
Chain | Residue |
B | PRO243 |
B | ILE244 |
B | VAL245 |
B | LYS263 |
B | TRP426 |
B | TYR427 |
B | GLN428 |
site_id | BC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE DMS B 508 |
Chain | Residue |
B | GLN242 |
B | TYR271 |
B | ASN348 |
B | HOH642 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 3 |
Details | BINDING: |
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 |
Chain | Residue | Details |
B | TRP401 | |
B | TRP414 | |
A | ASP498 | |
A | ASP549 | |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: Essential for RT p66/p51 heterodimerization |
Chain | Residue | Details |
A | TRP401 | |
A | TRP414 | |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | SITE: Cleavage; by viral protease; partial |
Chain | Residue | Details |
A | PHE440 | |