2AVV
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, D, E | Pol polyprotein | polymer | 99 | 10770.7 | 4 | UniProt (P04587) Pfam (PF00077) In PDB | Human immunodeficiency virus 1 | HIV-1 PROTEASE |
| 2 | A, E | 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 | 2 | Chemie (MK1) | |||
| 3 | A, B, E | ACETIC ACID | non-polymer | 60.1 | 3 | Chemie (ACY) | |||
| 4 | B, D | CHLORIDE ION | non-polymer | 35.5 | 2 | Chemie (CL) | |||
| 5 | water | water | 18.0 | 380 | Chemie (HOH) |
Sequence modifications
A, B, D, E: 1 - 99 (UniProt: P04587)
| PDB | External Database | Details |
|---|---|---|
| Lys 7 | Gln 75 | engineered mutation |
| Ile 33 | Leu 101 | engineered mutation |
| Ile 63 | Leu 131 | engineered mutation |
| Ala 67 | Cys 135 | engineered mutation |
| Ser 73 | Gly 141 | engineered mutation |
| Ala 95 | Cys 163 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 4 |
| Total formula weight | 43082.8 | |
| Non-Polymers* | Number of molecules | 7 |
| Total formula weight | 1478.6 | |
| All* | Total formula weight | 44561.4 |
