› 9b2h

X-ray diffraction
1.32Å resolution

HIV-1 wild type protease with GRL-072-17A, a substituted tetrahydrofuran derivative based on Darunavir as P2 group

Released:
DOI: 10.2210/pdb9b2h/pdb
PDB entry 9b2h coloured by chain, front view.
PDB entry 9b2h coloured by chain, side view.
PDB entry 9b2h coloured by chain, top view.
Source organism: Human immunodeficiency virus 1
Primary publication:
Design of substituted tetrahydrofuran derivatives for HIV-1 protease inhibitors: synthesis, biological evaluation, and X-ray structural studies.
Ghosh AK, Lee D, Sharma A, Johnson ME, Ghosh AK, Wang YF, Agniswamy J, Amano M, Hattori SI, Weber IT, Mitsuya H
Org Biomol Chem (2024)
PMID: 38973505

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:
PDBe Complex ID:
PDB-CPX-181991 (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: 10.74 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q7SSI0 (Residues: 1-99; Coverage: 100%)
Gene name: pol
Sequence domains: Retroviral aspartyl protease

Ligands and Environments

5 bound ligands:
Ligand NA 2 x NA
Ligand CL 4 x CL
Ligand GOL 2 x GOL
Ligand FMT 1 x FMT
Ligand A1AIH 1 x A1AIH
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P21212
Unit cell:
a: 58.576Å b: 85.877Å c: 46.312Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.132 0.13 0.164
Expression system: Escherichia coli BL21(DE3)

Quick links