3u71

X-ray diffraction
2.72Å resolution

Crystal Structure Analysis of South African wild type HIV-1 Subtype C Protease

Released:
Entry authors: Naicker P, Fanucchi S, Achilonu IA, Fernandes MA, Dirr HW, Sayed Y

Function and Biology Details

Reactions catalysed:
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1)
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.
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protease Chain: A
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 10.77 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q994Q3 (Residues: 59-157; Coverage: 23%)
Gene name: pol
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER AXS MICROSTAR
Spacegroup: P41212
Unit cell:
a: 45.928Å b: 45.928Å c: 99.96Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.217 0.283
Expression system: Escherichia coli BL21(DE3)