Function and Biology Details
Reaction catalysed:
Specific for a P1 residue that is hydrophobic, and P1' variable, but often Pro.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Peptidase A2 domain-containing protein (preferred)
PDBe Complex ID:
PDB-CPX-192967 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Peptidase A2 domain-containing protein
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 10.8 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases
Length: 99 amino acids
Theoretical weight: 10.8 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
Q9Q2G8 (Residues: 1-99; Coverage: 100%)
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases
Peptidase A2 domain-containing protein
Molecule details ›
Chain: B
Length: 99 amino acids
Theoretical weight: 10.88 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases
Length: 99 amino acids
Theoretical weight: 10.88 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: Q9Q288 (Residues: 1-99; Coverage: 100%)
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases
