1RTD
STRUCTURE OF A CATALYTIC COMPLEX OF HIV-1 REVERSE TRANSCRIPTASE: IMPLICATIONS FOR NUCLEOSIDE ANALOG DRUG RESISTANCE
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 | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 600 |
| Chain | Residue |
| A | ASP110 |
| A | VAL111 |
| A | ASP185 |
| A | MG601 |
| A | TTP700 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 601 |
| Chain | Residue |
| F | DG22 |
| A | ASP110 |
| A | ASP185 |
| A | MG600 |
| A | TTP700 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 602 |
| Chain | Residue |
| A | ASP443 |
| A | ASP498 |
| A | ASP549 |
| A | MG605 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 603 |
| Chain | Residue |
| C | ASP110 |
| C | VAL111 |
| C | ASP185 |
| C | MG604 |
| C | TTP705 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 604 |
| Chain | Residue |
| C | ASP110 |
| C | ASP185 |
| C | MG603 |
| C | TTP705 |
| H | DG22 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 605 |
| Chain | Residue |
| A | ASP549 |
| A | MG602 |
| site_id | AC7 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE TTP A 700 |
| Chain | Residue |
| A | LYS65 |
| A | ARG72 |
| A | ASP110 |
| A | VAL111 |
| A | GLY112 |
| A | ASP113 |
| A | ALA114 |
| A | TYR115 |
| A | GLN151 |
| A | ASP185 |
| A | MG600 |
| A | MG601 |
| E | DA5 |
| F | DG22 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE TTP C 705 |
| Chain | Residue |
| C | LYS65 |
| C | ARG72 |
| C | VAL111 |
| C | GLY112 |
| C | ASP113 |
| C | ALA114 |
| C | TYR115 |
| C | GLN151 |
| C | ASP185 |
| C | MG603 |
| C | MG604 |
| G | DA5 |
| H | DG22 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 34 |
| Details | ZN_FING: CCHC-type 1 => ECO:0000255|PROSITE-ProRule:PRU00047 |
| Chain | Residue | Details |
| B | HIS235-TRP252 | |
| D | HIS235-TRP252 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 34 |
| Details | ZN_FING: CCHC-type 2 => ECO:0000255|PROSITE-ProRule:PRU00047 |
| Chain | Residue | Details |
| B | ASP256-GLY273 | |
| D | ASP256-GLY273 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | ACT_SITE: For protease activity; shared with dimeric partner => ECO:0000255|PROSITE-ProRule:PRU10094, ECO:0000305|PubMed:33542150 |
| Chain | Residue | Details |
| B | ARG358 | |
| D | ARG358 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Cis/trans isomerization of proline peptide bond; by human PPIA/CYPA |
| Chain | Residue | Details |
| B | LYS66 | |
| D | LYS66 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | SITE: Cleavage; by viral protease => ECO:0000250 |
| Chain | Residue | Details |
| B | HIS208 | |
| B | GLN222 | |
| B | GLY285 | |
| B | GLU432 | |
| D | HIS208 | |
| D | GLN222 | |
| D | GLY285 | |
| D | GLU432 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | SITE: Cleavage; by viral protease => ECO:0000255 |
| Chain | Residue | Details |
| B | LYS238 | |
| B | TYR271 | |
| B | ARG277 | |
| D | LYS238 | |
| D | TYR271 | |
| D | ARG277 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by viral protease => ECO:0000305|PubMed:15183348 |
| Chain | Residue | Details |
| B | GLY333 | |
| D | GLY333 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | SITE: Cleavage; by viral protease |
| Chain | Residue | Details |
| A | GLY273 | |
| A | GLY333 | |
| C | GLY273 | |
| C | GLY333 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by viral protease => ECO:0000269|PubMed:2476069 |
| Chain | Residue | Details |
| A | GLU432 | |
| C | GLU432 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 4 |
| 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 |
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 |
| A | ASP186 | metal ligand |
| A | LYS220 | proton donor |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 175 |
| Chain | Residue | Details |
| D | ARG358 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| D | GLY359 | electrostatic stabiliser, transition state stabiliser |
| D | ALA360 | electrostatic stabiliser, hydrogen bond donor |
