4Q1Y
Mutations Outside the Active Site of HIV-1 Protease Alter Enzyme Structure and Dynamic Ensemble of the Active Site to Confer Drug Resistance
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) | aspartyl protease | polymer | 99 | 10863.8 | 2 | UniProt (V5Y949) Pfam (PF00077) UniProt (by SIFTS) (P04585) | Human immunodeficiency virus 1 | Pol protein |
| 2 | C, D, E (A) | PHOSPHATE ION | non-polymer | 95.0 | 3 | Chemie (PO4) | |||
| 3 | F, G, I (A, B) | ACETATE ION | non-polymer | 59.0 | 3 | Chemie (ACT) | |||
| 4 | H (A) | (3R,3AS,6AR)-HEXAHYDROFURO[2,3-B]FURAN-3-YL(1S,2R)-3-[[(4-AMINOPHENYL)SULFONYL](ISOBUTYL)AMINO]-1-BENZYL-2-HYDROXYPROPYLCARBAMATE | non-polymer | 547.7 | 1 | Chemie (017) | |||
| 5 | J, K (A, B) | water | water | 18.0 | 124 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 99 (UniProt: V5Y949)
| PDB | External Database | Details |
|---|---|---|
| Lys 7 | Gln 7 | engineered mutation |
| Ile 32 | Val 32 | engineered mutation |
| Phe 33 | Leu 33 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 21727.7 | |
| Non-Polymers* | Number of molecules | 7 |
| Total formula weight | 1009.7 | |
| All* | Total formula weight | 22737.4 |
