4Q1W
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 | ASPARTYL PROTEASE | polymer | 99 | 10833.8 | 2 | UniProt (V5Y949) Pfam (PF00077) UniProt (by SIFTS) (P04585) In PDB | Human immunodeficiency virus 1 | Pol protein |
2 | A, B | PHOSPHATE ION | non-polymer | 95.0 | 4 | Chemie (PO4) | |||
3 | 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) | |||
4 | B | ACETATE ION | non-polymer | 59.0 | 1 | Chemie (ACT) | |||
5 | water | water | 18.0 | 109 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 99 (UniProt: V5Y949)
PDB | External Database | Details |
---|---|---|
Lys 7 | Gln 7 | engineered mutation |
Met 90 | Leu 90 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
Polymers | Number of chains | 2 |
Total formula weight | 21667.7 | |
Non-Polymers* | Number of molecules | 6 |
Total formula weight | 986.6 | |
All* | Total formula weight | 22654.2 |