› 2a4f

X-ray diffraction
1.9Å resolution

Synthesis and Activity of N-Axyl Azacyclic Urea HIV-1 Protease Inhibitors with High Potency Against Multiple Drug Resistant Viral Strains.

Released:
DOI: 10.2210/pdb2a4f/pdb
PDB entry 2a4f coloured by chain, front view.
PDB entry 2a4f coloured by chain, side view.
PDB entry 2a4f coloured by chain, top view.
Source organism: Human immunodeficiency virus 1
Primary publication:
Synthesis and activity of N-acyl azacyclic urea HIV-1 protease inhibitors with high potency against multiple drug resistant viral strains.
Zhao C, Sham HL, Sun M, Stoll VS, Stewart KD, Lin S, Mo H, Vasavanonda S, Saldivar A, Park C, McDonald EJ, Marsh KC, Klein LL, Kempf DJ, Norbeck DW
Bioorg Med Chem Lett 15 5499-503 (2005)
PMID: 16203141

Function and Biology Details

Reaction catalysed: 
Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192969 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase A2 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 99 amino acids
Theoretical weight: 10.8 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9Q2G8 (Residues: 1-99; Coverage: 100%)
Gene name: ORF
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P21212
Unit cell:
a: 58.008Å b: 85.742Å c: 46.646Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.298 0.298 0.336
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Tetrahydrofuran, tetrahydropyran, triazoles and related heterocyclic derivatives as HIV protease inhibitors.
Ghosh et al. (2011)
1 more

2 mentions without citation

Recent Progress in the Development of HIV-1 Protease Inhibitors for the Treatment of HIV/AIDS.
Ghosh et al. (2016)
1 more