1HMV
THE STRUCTURE OF UNLIGANDED REVERSE TRANSCRIPTASE FROM THE HUMAN IMMUNODEFICIENCY VIRUS TYPE 1
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 |
| E | 0003676 | molecular_function | nucleic acid binding |
| E | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
| E | 0004523 | molecular_function | RNA-DNA hybrid ribonuclease activity |
| E | 0006278 | biological_process | RNA-templated DNA biosynthetic process |
| F | 0003964 | molecular_function | RNA-directed DNA polymerase activity |
| F | 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 501 |
| Chain | Residue |
| A | ASP443 |
| A | GLU478 |
| A | ASP498 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG D 501 |
| Chain | Residue |
| C | ASP443 |
| C | GLU478 |
| C | ASP498 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG F 501 |
| Chain | Residue |
| E | ASP443 |
| E | GLU478 |
| E | ASP498 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG H 501 |
| Chain | Residue |
| G | ASP443 |
| G | GLU478 |
| G | ASP498 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 68 |
| Details | ZN_FING: CCHC-type 1 => ECO:0000255|PROSITE-ProRule:PRU00047 |
| Chain | Residue | Details |
| B | LYS223-THR240 | |
| D | LYS223-THR240 | |
| F | LYS223-THR240 | |
| H | LYS223-THR240 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 68 |
| Details | ZN_FING: CCHC-type 2 => ECO:0000255|PROSITE-ProRule:PRU00047 |
| Chain | Residue | Details |
| B | ILE244-VAL261 | |
| D | ILE244-VAL261 | |
| F | ILE244-VAL261 | |
| H | ILE244-VAL261 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | ACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000269|PubMed:12924029 |
| Chain | Residue | Details |
| B | ARG358 | |
| D | ARG358 | |
| F | ARG358 | |
| H | ARG358 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | SITE: Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA => ECO:0000250 |
| Chain | Residue | Details |
| B | ASN54 | |
| D | ASN54 | |
| F | ASN54 | |
| H | ASN54 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | SITE: Cleavage; by viral protease => ECO:0000250 |
| Chain | Residue | Details |
| B | GLY196 | |
| B | LEU210 | |
| D | GLY196 | |
| D | LEU210 | |
| F | GLY196 | |
| F | LEU210 | |
| H | GLY196 | |
| H | LEU210 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | SITE: Cleavage; by viral protease => ECO:0000255 |
| Chain | Residue | Details |
| B | ASN265 | |
| D | ASN265 | |
| F | ASN265 | |
| H | ASN265 | |
| E | GLY196 | |
| E | LEU210 | |
| G | GLY196 | |
| G | LEU210 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | SITE: Cleavage; by viral protease |
| Chain | Residue | Details |
| B | GLY273 | |
| B | GLY333 | |
| D | GLY273 | |
| D | GLY333 | |
| F | GLY273 | |
| F | GLY333 | |
| H | GLY273 | |
| H | GLY333 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | SITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069 |
| Chain | Residue | Details |
| B | GLU432 | |
| D | GLU432 | |
| F | GLU432 | |
| H | GLU432 | |
| E | GLY273 | |
| E | GLY333 | |
| G | GLY273 | |
| G | GLY333 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 8 |
| Details | MOD_RES: Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 => ECO:0000269|PubMed:17415034 |
| Chain | Residue | Details |
| B | LYS220 | |
| B | GLN242 | |
| D | LYS220 | |
| D | GLN242 | |
| F | LYS220 | |
| F | GLN242 | |
| H | LYS220 | |
| H | GLN242 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 8 |
| Details | MOD_RES: Asymmetric dimethylarginine; in Nucleocapsid protein p7; by host PRMT6 => ECO:0000269|PubMed:17415034 |
| Chain | Residue | Details |
| A | LYS220 | |
| A | GLN242 | |
| C | LYS220 | |
| C | GLN242 | |
| E | LYS220 | |
| E | GLN242 | |
| G | LYS220 | |
| G | GLN242 |
