2AVO
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 | 10740.7 | 2 | UniProt (P04587) Pfam (PF00077) UniProt (by SIFTS) (Q7SSI0) In PDB | Human immunodeficiency virus 1 | |
| 2 | A | SULFATE ION | non-polymer | 96.1 | 1 | Chemie (SO4) | HIV-1 PROTEASE | ||
| 3 | A | DIMETHYL SULFOXIDE | non-polymer | 78.1 | 1 | Chemie (DMS) | |||
| 4 | B | N-[2(R)-HYDROXY-1(S)-INDANYL]-5-[(2(S)-TERTIARY BUTYLAMINOCARBONYL)-4(3-PYRIDYLMETHYL)PIPERAZINO]-4(S)-HYDROXY-2(R)-PHENYLMETHYLPENTANAMIDE | non-polymer | 613.8 | 1 | Chemie (MK1) | |||
| 5 | B | ACETIC ACID | non-polymer | 60.1 | 2 | Chemie (ACY) | |||
| 6 | B | GLYCEROL | non-polymer | 92.1 | 1 | Chemie (GOL) | |||
| 7 | water | water | 18.0 | 264 | 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 | 6 |
| Total formula weight | 1000.2 | |
| All* | Total formula weight | 22481.5 |
