Structure analysis

Viability of a drug-resistant HIV-1 protease mutant: structural insights for better antiviral therapy

X-ray diffraction
1.9Å resolution
Assembly composition:
hetero trimer (preferred)
Entry contents: 2 distinct polypeptide molecules

Assemblies

Assembly 1 (preferred)
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Multimeric state: hetero trimer
Accessible surface area: 9299.4 Å2
Buried surface area: 6182.32 Å2
Dissociation area: 852.15 Å2
Dissociation energy (ΔGdiss): 7.91 kcal/mol
Dissociation entropy (TΔSdiss): 6.58 kcal/mol
Symmetry number: 1
PDBe Complex ID: PDB-CPX-136902

Macromolecules

Chains: A, B
Length: 99 amino acids
Theoretical weight: 10.77 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
UniProt:
  • Canonical: P03369 (Residues: 491-589; Coverage: 7%)
Gene name: gag-pol
Pfam: Retroviral aspartyl protease
InterPro:
CATH: Acid Proteases
SCOP: Retroviral protease (retropepsin)

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Chain: P
Length: 10 amino acids
Theoretical weight: 1.16 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Not provided
UniProt:
  • Canonical: Q9YYH6 (Residues: 104-113; Coverage: 7%)
Gene name: gag

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