2B60
Structure of HIV-1 protease mutant bound to Ritonavir
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B (A, B) | Gag-Pol polyprotein | polymer | 99 | 10863.8 | 2 | UniProt (Q7SMT3) | Human immunodeficiency virus 1 | |
| 2 | C (A) | GLYCEROL | non-polymer | 92.1 | 1 | Chemie (GOL) PubChem (753) | |||
| 3 | D (B) | RITONAVIR | non-polymer | 720.9 | 1 | BIRD (PRD_001001) Chemie (RIT) PubChem (5076) PubChem (16760215) PubChem (44325718) PubChem (60954) PubChem (45266310) PubChem (53487909) PubChem (54103495) PubChem (58662536) PubChem (392622) PubChem (66509020) PubChem (72942039) PubChem (72942040) PubChem (90717239) PubChem (455315) PubChem (92402731) PubChem (93535511) PubChem (93535509) PubChem (9853294) PubChem (93535510) PubChem (135172324) PubChem (123133890) PubChem (10395099) PubChem (133662525) PubChem (134602828) PubChem (134751724) PubChem (141861627) PubChem (169446189) PubChem (169446190) PubChem (170130299) | |||
| 4 | E, F (A, B) | water | water | 18.0 | 75 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 99 (UniProt: Q7SMT3)
| PDB | External Database | Details |
|---|---|---|
| Arg 20 | Lys 519 | engineered mutation |
| Ile 32 | Val 531 | engineered mutation |
| Phe 33 | Leu 532 | engineered mutation |
| Ile 36 | Met 535 | engineered mutation |
| Pro 63 | Leu 562 | engineered mutation |
| Val 71 | Ala 570 | engineered mutation |
| Ala 82 | Val 581 | engineered mutation |
| Met 90 | Leu 589 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 21727.5 | |
| Non-Polymers* | Number of molecules | 2 |
| Total formula weight | 813.0 | |
| All* | Total formula weight | 22540.6 |
