PDBe 2nmz

X-ray diffraction
0.97Å resolution

Crystal structure analysis of HIV-1 protease mutant V82A with a inhibitor saquinavir

Released:

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

Structure analysis Details

Assembly composition:
homo dimer (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: 10.71 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7SSI0 (Residues: 1-99; Coverage: 100%)
Gene name: pol
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 51.131Å b: 58.588Å c: 61.61Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.128 0.127 0.144
Expression system: Escherichia coli BL21(DE3)