PDBe 1hrh

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF THE RIBONUCLEASE H DOMAIN OF HIV-1 REVERSE TRANSCRIPTASE

Released:

Function and Biology Details

Reactions catalysed:
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. 
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). 
Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro. 
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid. 
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
p15 Chains: A, B
Molecule details ›
Chains: A, B
Length: 136 amino acids
Theoretical weight: 15.03 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Not provided
UniProt:
  • Canonical: P03366 (Residues: 1026-1161; Coverage: 9%)
Gene name: gag-pol
Sequence domains: RNase H
Structure domains: Nucleotidyltransferase; domain 5

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P31
Unit cell:
a: 51.9Å b: 51.9Å c: 114.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.2 not available not available
Expression system: Not provided