› 4yoa

X-ray diffraction
1.7Å resolution

Crsystal structure HIV-1 Protease MDR769 L33F Complexed with darunavir

Released:
DOI: 10.2210/pdb4yoa/pdb
PDB entry 4yoa coloured by chain, front view.
PDB entry 4yoa coloured by chain, side view.
PDB entry 4yoa coloured by chain, top view.
Source organism: Human immunodeficiency virus 1
Primary publication:
The L33F darunavir resistance mutation acts as a molecular anchor reducing the flexibility of the HIV-1 protease 30s and 80s loops.
Kuiper BD, Keusch BJ, Dewdney TG, Chordia P, Ross K, Brunzelle JS, Kovari IA, MacArthur R, Salimnia H, Kovari LC
Biochem Biophys Rep 2 160-165 (2015)
PMID: 29124158

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-177789 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase A2 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 10.8 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5RTL1 (Residues: 1-99; Coverage: 100%)
Gene name: pol
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:
Ligand 017 1 x 017
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P41212
Unit cell:
a: 45.47Å b: 45.47Å c: 102.22Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.19 0.225
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Increased activity of unlinked Zika virus NS2B/NS3 protease compared to linked Zika virus protease.
Kuiper et al. (2017)
3 more

1 mention without citation

The L33F darunavir resistance mutation acts as a molecular anchor reducing the flexibility of the HIV-1 protease 30s and 80s loops.
Kuiper et al. (2015)