2AVM
Kinetics, stability, and structural changes in high resolution crystal structures of HIV-1 protease with drug resistant mutations L24I, I50V, AND G73S
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) | HIV-1 protease | polymer | 99 | 10740.7 | 2 | UniProt (P04587) Pfam (PF00077) | Human immunodeficiency virus 1 | HIV-1 PROTEASE |
| 2 | C, F, G (A, B) | GLYCEROL | non-polymer | 92.1 | 3 | Chemie (GOL) | |||
| 3 | D (B) | N-{(2S)-2-[(N-acetyl-L-threonyl-L-isoleucyl)amino]hexyl}-L-norleucyl-L-glutaminyl-N~5~-[amino(iminio)methyl]-L-ornithinamide | non-polymer | 771.0 | 1 | BIRD (PRD_000398) Chemie (2NC) | |||
| 4 | E (B) | ACETIC ACID | non-polymer | 60.1 | 1 | Chemie (ACY) | |||
| 5 | H, I (A, B) | water | water | 18.0 | 345 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 99 (UniProt: P04587)
| PDB | External Database | Details |
|---|---|---|
| Lys 7 | Gln 75 | engineered mutation |
| Ile 24 | Leu 92 | engineered mutation |
| Ile 33 | Leu 101 | engineered mutation |
| Ile 63 | Leu 131 | engineered mutation |
| Ala 67 | Cys 135 | engineered mutation |
| Ala 95 | Cys 163 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 21481.4 | |
| Non-Polymers* | Number of molecules | 5 |
| Total formula weight | 1107.3 | |
| All* | Total formula weight | 22588.7 |
