1e0e

Solution NMR

N-terminal zinc-binding HHCC domain of HIV-2 integrase

Released:

Function and Biology Details

Reactions catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
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.
Endopeptidase for which the P1 residue is preferably hydrophobic.
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137999 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Integrase Chains: A, B
Molecule details ›
Chains: A, B
Length: 55 amino acids
Theoretical weight: 6.27 KDa
Source organism: Human immunodeficiency virus type 2 (ISOLATE ROD)
Expression system: Escherichia coli
UniProt:
  • Canonical: P04584 (Residues: 1172-1226; Coverage: 4%)
Gene name: gag-pol
Sequence domains: Integrase Zinc binding domain
Structure domains: Arc Repressor Mutant, subunit A

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 84%
Refinement method: simulated annealing
Expression system: Escherichia coli