2AVQ
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 | Pol polyprotein | polymer | 99 | 10726.6 | 2 | UniProt (P04587) Pfam (PF00077) In PDB | Human immunodeficiency virus type 1 (BH5 ISOLATE) | HIV-1 PROTEASE |
| 2 | A | DIMETHYL SULFOXIDE | non-polymer | 78.1 | 1 | Chemie (DMS) | |||
| 3 | A, B | GLYCEROL | non-polymer | 92.1 | 2 | Chemie (GOL) | |||
| 4 | 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) | |||
| 5 | water | water | 18.0 | 333 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 99 (UniProt: P04587)
| PDB | External Database | Details |
|---|---|---|
| Lys 7 | Gln 75 | engineered mutation |
| Ile 33 | Leu 101 | engineered mutation |
| Val 50 | Ile 118 | 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 | 21453.3 | |
| Non-Polymers* | Number of molecules | 4 |
| Total formula weight | 1033.3 | |
| All* | Total formula weight | 22486.6 |
