3BXR
Crystal Structures Of Highly Constrained Substrate And Hydrolysis Products Bound To HIV-1 Protease. Implications For Catalytic Mechanism
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) | Protease | polymer | 99 | 10764.7 | 2 | UniProt (P03369) Pfam (PF00077) | Retropepsin, PR | |
| 2 | C, D, E, F (A, B) | SULFATE ION | non-polymer | 96.1 | 4 | Chemie (SO4) | |||
| 3 | G (B) | (9S,12S)-9-(1-methylethyl)-N-[(8S,11S)-8-[(1S)-1-methylpropyl]-7,10-dioxo-2-oxa-6,9-diazabicyclo[11.2.2]heptadeca-1(15),13,16-trien-11-yl]-7,10-dioxo-2-oxa-8,11-diazabicyclo[12.2.2]octadeca-1(16),14,17-triene-12-carboxamide | non-polymer | 677.8 | 1 | Chemie (DRR) | |||
| 4 | H, I (A, B) | water | water | 18.0 | 207 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 99 (UniProt: P03369)
| PDB | External Database | Details |
|---|---|---|
| Lys 7 | Gln 497 | engineered mutation |
| Asn 25 | Asp 515 | engineered mutation |
| Ile 33 | Leu 523 | engineered mutation |
| Aba 67 | Cys 557 | engineered mutation |
| Aba 95 | Cys 585 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 21529.4 | |
| Non-Polymers* | Number of molecules | 5 |
| Total formula weight | 1062.1 | |
| All* | Total formula weight | 22591.5 |
