3ao4

X-ray diffraction
1.95Å resolution

Fragment-based approach to the design of ligands targeting a novel site on HIV-1 integrase

Released:

Function and Biology Details

Reactions catalysed:
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180777 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
POL polyprotein Chains: A, B
Molecule details ›
Chains: A, B
Length: 163 amino acids
Theoretical weight: 17.77 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q72498 (Residues: 765-927; Coverage: 16%)
Gene name: pol
Sequence domains: Integrase core domain
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P32
Unit cell:
a: 48.2Å b: 48.2Å c: 103.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.205 0.203 0.253
Expression system: Escherichia coli