8tck

X-ray diffraction
2.2Å resolution

Apo crystal Structure of modified HIV reverse transcriptase p51 domain (FPC1)

Released:
Entry authors: Pedersen LC, London RE

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.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-247180 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
p51 RT Chain: B
Molecule details ›
Chain: B
Length: 343 amino acids
Theoretical weight: 39.85 KDa
Source organism: HIV whole-genome vector AA1305#18
Expression system: Escherichia coli
UniProt:
  • Canonical: P04585 (Residues: 588-1005; Coverage: 23%)
Gene name: gag-pol
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 53.735Å b: 63.952Å c: 128.296Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.208 0.24
Expression system: Escherichia coli