2g69

X-ray diffraction
1.35Å resolution

Structure of Unliganded HIV-1 Protease F53L Mutant

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 Chain: A
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 10.71 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7SSI0 (Residues: 1-99; Coverage: 100%)
Gene name: pol
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P41212
Unit cell:
a: 60.946Å b: 60.946Å c: 55.551Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.155 0.234
Expression system: Escherichia coli