3BXS
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 | Protease | polymer | 99 | 10765.7 | 2 | UniProt (P03369) Pfam (PF00077) In PDB | Retropepsin, PR | |
2 | A, B | SULFATE ION | non-polymer | 96.1 | 3 | Chemie (SO4) | |||
3 | A, B | (9S,12S)-9-(1-methylethyl)-7,10-dioxo-2-oxa-8,11-diazabicyclo[12.2.2]octadeca-1(16),14,17-triene-12-carboxylic acid | non-polymer | 362.4 | 2 | Chemie (DRS) | |||
4 | water | water | 18.0 | 201 | Chemie (HOH) |
Sequence modifications
A, B: 1 - 99 (UniProt: P03369)
PDB | External Database | Details |
---|---|---|
Lys 7 | Gln 497 | 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 | 21531.4 | |
Non-Polymers* | Number of molecules | 5 |
Total formula weight | 1013.0 | |
All* | Total formula weight | 22544.4 |