1RTD
STRUCTURE OF A CATALYTIC COMPLEX OF HIV-1 REVERSE TRANSCRIPTASE: IMPLICATIONS FOR NUCLEOSIDE ANALOG DRUG RESISTANCE
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, C (E, G) | DNA TEMPLATE FOR REVERSE TRANSCRIPTASE | polymer | 27 | 8327.4 | 2 | |||
| 2 | B, D (F, H) | DNA PRIMER FOR REVERSE TRANSCRIPTASE | polymer | 21 | 6416.1 | 2 | |||
| 3 | E, G (A, C) | PROTEIN (REVERSE TRANSCRIPTASE) | polymer | 554 | 63869.1 | 2 | UniProt (P03366) Pfam (PF00078) Pfam (PF06817) Pfam (PF06815) Pfam (PF00075) | Human immunodeficiency virus 1 | HIV-1 RT |
| 4 | F, H (B, D) | PROTEIN (REVERSE TRANSCRIPTASE) | polymer | 440 | 51399.0 | 2 | UniProt (P04585) Pfam (PF00078) Pfam (PF06817) Pfam (PF06815) | Human immunodeficiency virus 1 | HIV-1 RT |
| 5 | I, J, K, L, N... (A, C) | MAGNESIUM ION | non-polymer | 24.3 | 6 | Chemie (MG) | |||
| 6 | M, P (A, C) | THYMIDINE-5'-TRIPHOSPHATE | non-polymer | 482.2 | 2 | Chemie (TTP) |
Sequence modifications
A, C: 1 - 554 (UniProt: P03366)
| PDB | External Database | Details |
|---|---|---|
| Lys 1 | Pro 168 | engineered mutation |
| Arg 172 | Lys 339 | conflict |
| Cys 258 | Gln 425 | engineered mutation |
| Asp 471 | Asn 638 | conflict |
| Gln 478 | Glu 645 | engineered mutation |
| Glu 512 | Lys 629 | conflict |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 8 |
| Total formula weight | 260023.4 | |
| Non-Polymers* | Number of molecules | 8 |
| Total formula weight | 1110.2 | |
| All* | Total formula weight | 261133.5 |
