1hmv

X-ray diffraction
3.2Å resolution

THE STRUCTURE OF UNLIGANDED REVERSE TRANSCRIPTASE FROM THE HUMAN IMMUNODEFICIENCY VIRUS TYPE 1

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-136840 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Reverse transcriptase/ribonuclease H Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 560 amino acids
Theoretical weight: 64.52 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
UniProt:
  • Canonical: P03366 (Residues: 600-1159; Coverage: 39%)
Gene name: gag-pol
Sequence domains:
Structure domains:
p51 RT Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 440 amino acids
Theoretical weight: 51.37 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
UniProt:
  • Canonical: P03366 (Residues: 600-1039; Coverage: 30%)
Gene name: gag-pol
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 168.7Å b: 162.8Å c: 331.8Å
α: 90° β: 105.7° γ: 90°
R-values:
R R work R free
0.254 0.254 0.297
Expression system: Escherichia coli