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:
homo dimer (preferred)
Assembly name:
Peptidase A2 domain-containing protein, Protease (preferred)
PDBe Complex ID:
PDB-CPX-181991 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase A2 domain-containing protein
Molecule details ›
Chain: A
Length: 99 amino acids
Theoretical weight: 10.71 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
UniProt:
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases
Length: 99 amino acids
Theoretical weight: 10.71 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
UniProt:
- Canonical:
Q7SSI0 (Residues: 1-99; Coverage: 100%)
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
APS BEAMLINE 22-ID
Spacegroup:
P41212
Expression system: Escherichia coli
