4fae

X-ray diffraction
2.3Å resolution

Substrate p2/NC in Complex with a Human Immunodeficiency Virus Type 1 Protease Variant

Released:

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:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-169396 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Pol protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 99 amino acids
Theoretical weight: 10.77 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
UniProt:
  • Canonical: Q000H7 (Residues: 1-99; Coverage: 25%)
Gene name: pol
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases
Substrate p2/NC peptide Chain: D
Molecule details ›
Chain: D
Length: 7 amino acids
Theoretical weight: 837 Da
Source organism: Human immunodeficiency virus 1
Expression system: Not provided
UniProt:
  • Canonical: Q9YP46 (Residues: 375-381; Coverage: 1%)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P212121
Unit cell:
a: 28.615Å b: 63.851Å c: 91.113Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.2 0.279
Expression systems:
  • Escherichia coli
  • Not provided