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 | 4 |
Details | BINDING SITE FOR RESIDUE MG A 600 |
Chain | Residue |
A | ASP110 |
A | VAL111 |
A | ASP185 |
A | TNV823 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE MG A 601 |
Chain | Residue |
A | ASP443 |
A | ASP498 |
site_id | AC3 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE TNV A 823 |
Chain | Residue |
A | VAL111 |
A | GLY112 |
A | ASP113 |
A | ALA114 |
A | GLN151 |
A | ASP185 |
A | LYS219 |
A | MG600 |
P | DDG822 |
T | DT705 |
T | DC706 |
A | LYS65 |
A | ARG72 |
A | ASP110 |
site_id | AC4 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 824 |
Chain | Residue |
A | LYS101 |
A | LYS103 |
A | VAL106 |
A | TYR188 |
A | HIS235 |
A | PRO236 |
A | TYR318 |
A | HOH827 |
site_id | AC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 825 |
Chain | Residue |
A | GLU328 |
A | GLN340 |
A | TYR342 |
A | PRO345 |
A | GOL826 |
A | HOH829 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE GOL A 826 |
Chain | Residue |
A | GLN330 |
A | GLN340 |
A | GOL825 |
site_id | AC7 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 438 |
Chain | Residue |
B | ASP76 |
B | ARG78 |
B | GLU79 |
B | LYS82 |
B | GLU413 |
B | GOL439 |
site_id | AC8 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE GOL B 439 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
B | HIS235-TRP252 | |
Chain | Residue | Details |
B | ASP256-GLY273 | |
Chain | Residue | Details |
B | ARG358 | |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
B | ASP110 | |
B | ASP185 | |
B | ASP186 | |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | SITE: Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA |
Chain | Residue | Details |
B | LYS66 | |
site_id | SWS_FT_FI6 |
Number of Residues | 3 |
Details | SITE: Cleavage; by viral protease => ECO:0000250 |
Chain | Residue | Details |
B | HIS208 | |
B | GLN222 | |
B | GLY285 | |
site_id | SWS_FT_FI7 |
Number of Residues | 3 |
Details | SITE: Cleavage; by viral protease => ECO:0000255 |
Chain | Residue | Details |
B | LYS238 | |
B | TYR271 | |
B | ARG277 | |
Chain | Residue | Details |
B | GLY333 | |
A | GLY333 | |
site_id | SWS_FT_FI9 |
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_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 => ECO:0000269|PubMed:17415034 |
Chain | Residue | Details |
A | LYS220 | |
A | GLN242 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 175 |
Chain | Residue | Details |
B | ARG358 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | GLY359 | electrostatic stabiliser, transition state stabiliser |
B | ALA360 | electrostatic stabiliser, hydrogen bond donor |