› 1hvi

X-ray diffraction
1.8Å resolution

INFLUENCE OF STEREOCHEMISTRY ON ACTIVITY AND BINDING MODES FOR C2 SYMMETRY-BASED DIOL INHIBITORS OF HIV-1 PROTEASE

Released:
DOI: 10.2210/pdb1hvi/pdb
PDB entry 1hvi coloured by chain, front view.
PDB entry 1hvi coloured by chain, side view.
PDB entry 1hvi coloured by chain, top view.
Source organism: Human immunodeficiency virus 1
Primary publication:
Influence of Stereochemistry on Activity and Binding Modes for C2 Symmetry-Based Diol Inhibitors of HIV-1 Protease
Hosur MV, Bhat TN, Kempf D, Baldwin ET, Liu B, Gulnik S, Wideburg NE, Norbeck DW, Appelt K, Erickson JW
J. Am. Chem. Soc. 116 847-855 (1994)

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131646 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase A2 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 99 amino acids
Theoretical weight: 10.8 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli
UniProt:
  • Canonical: O92139 (Residues: 1-99; Coverage: 100%)
Gene name: pol
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:
Ligand A77 1 x A77
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 51.98Å b: 59.65Å c: 62.31Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 not available
Expression system: Escherichia coli

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Citations

6 mentions without citation

Reproducing crystal binding modes of ligand functional groups using Site-Identification by Ligand Competitive Saturation (SILCS) simulations.
Raman et al. (2011)
5 more