8ci7

X-ray diffraction
2.4Å resolution

Apo-crystal structure of a wild-type South African HIV-1 subtype C protease at 2.4 angstrom

Released:
Entry authors: Dlamini NP, Pandian R, Onisuru O, Achilonu IA, Sayed Y

Function and Biology Details

Reaction 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.
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189209 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Truncated pol polyprotein 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
UniProt:
  • Canonical: Q994Q3 (Residues: 59-157; Coverage: 23%)
Gene name: pol
Sequence domains: Retroviral aspartyl protease

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BRUKER IMUS 3.0 MICROFOCUS
Spacegroup: P41212
Unit cell:
a: 46.6Å b: 46.6Å c: 102.144Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.203 0.221
Expression system: Escherichia coli BL21