2hb2

X-ray diffraction
2.3Å resolution

Structure of HIV protease 6X mutant in apo form

Released:
Primary publication:
Conformational flexibility in the flap domains of ligand-free HIV protease.
Acta Crystallogr D Biol Crystallogr 63 866-75 (2007)
PMID: 17642513

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-190132 (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: 10.75 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9E3M8 (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: SSRL BEAMLINE BL1-5
Spacegroup: P41212
Unit cell:
a: 49.671Å b: 49.671Å c: 109.613Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.234 0.291
Expression system: Escherichia coli