1HVU
HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 REVERSE TRANSCRIPTASE COMPLEXED WITH A 33-BASE NUCLEOTIDE RNA PSEUDOKNOT
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 |
D | 0003676 | molecular_function | nucleic acid binding |
D | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
D | 0004523 | molecular_function | RNA-DNA hybrid ribonuclease activity |
D | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
E | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
E | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
G | 0003676 | molecular_function | nucleic acid binding |
G | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
G | 0004523 | molecular_function | RNA-DNA hybrid ribonuclease activity |
G | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
H | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
H | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
J | 0003676 | molecular_function | nucleic acid binding |
J | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
J | 0004523 | molecular_function | RNA-DNA hybrid ribonuclease activity |
J | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
K | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
K | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
Functional Information from PDB Data
site_id | PS2 |
Number of Residues | 3 |
Details |
Chain | Residue |
D | ASP110 |
D | ASP185 |
D | ASP186 |
site_id | PS3 |
Number of Residues | 3 |
Details |
Chain | Residue |
G | ASP110 |
G | ASP185 |
G | ASP186 |
site_id | PS4 |
Number of Residues | 3 |
Details |
Chain | Residue |
J | ASP110 |
J | ASP185 |
J | ASP186 |
site_id | PSE |
Number of Residues | 3 |
Details |
Chain | Residue |
A | ASP110 |
A | ASP185 |
A | ASP186 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: |
Chain | Residue | Details |
B | VAL111 | |
K | VAL111 | |
K | ASP186 | |
K | LEU187 | |
B | ASP186 | |
B | LEU187 | |
E | VAL111 | |
E | ASP186 | |
E | LEU187 | |
H | VAL111 | |
H | ASP186 | |
H | LEU187 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | SITE: Essential for RT p66/p51 heterodimerization |
Chain | Residue | Details |
B | TRP402 | |
G | LEU479 | |
G | SER499 | |
G | LYS550 | |
J | GLY444 | |
J | LEU479 | |
J | SER499 | |
J | LYS550 | |
B | GLU415 | |
E | TRP402 | |
E | GLU415 | |
H | TRP402 | |
H | GLU415 | |
K | TRP402 | |
K | GLU415 | |
G | GLY444 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069 |
Chain | Residue | Details |
A | PRO1 | |
D | PRO1 | |
G | PRO1 | |
J | PRO1 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | SITE: Essential for RT p66/p51 heterodimerization |
Chain | Residue | Details |
A | TRP402 | |
A | GLU415 | |
D | TRP402 | |
D | GLU415 | |
G | TRP402 | |
G | GLU415 | |
J | TRP402 | |
J | GLU415 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | SITE: Cleavage; by viral protease; partial |
Chain | Residue | Details |
A | TYR441 | |
D | TYR441 | |
G | TYR441 | |
J | TYR441 |