› 4njs

X-ray diffraction
1.8Å resolution

Crystal structure of multidrug-resistant clinical isolate A02 HIV-1 protease in complex with non-peptidic inhibitor, GRL008

Released:
DOI: 10.2210/pdb4njs/pdb
PDB entry 4njs coloured by chain, front view.
PDB entry 4njs coloured by chain, side view.
PDB entry 4njs coloured by chain, top view.
Source organism: Human immunodeficiency virus 1
Primary publication:
A conserved hydrogen-bonding network of P2 bis-tetrahydrofuran-containing HIV-1 protease inhibitors (PIs) with a protease active-site amino acid backbone aids in their activity against PI-resistant HIV.
Yedidi RS, Garimella H, Aoki M, Aoki-Ogata H, Desai DV, Chang SB, Davis DA, Fyvie WS, Kaufman JD, Smith DW, Das D, Wingfield PT, Maeda K, Ghosh AK, Mitsuya H
Antimicrob Agents Chemother 58 3679-88 (2014)
PMID: 24752271

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-191565 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase A2 domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 99 amino acids
Theoretical weight: 10.86 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9J006 (Residues: 1-99; Coverage: 100%)
Gene name: pol
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:
Ligand G08 2 x G08
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21
Unit cell:
a: 44.632Å b: 57.995Å c: 88.111Å
α: 90° β: 90.03° γ: 90°
R-values:
R R work R free
0.184 0.182 0.216
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

1 mention without citation

A conserved hydrogen-bonding network of P2 bis-tetrahydrofuran-containing HIV-1 protease inhibitors (PIs) with a protease active-site amino acid backbone aids in their activity against PI-resistant HIV.
Yedidi et al. (2014)