› 2o40

X-ray diffraction
1.65Å resolution

Crystal Structure of a Chemically Synthesized 203 Amino Acid 'Covalent Dimer' HIV-1 Protease Molecule

Released:
DOI: 10.2210/pdb2o40/pdb
PDB entry 2o40 coloured by chain, front view.
PDB entry 2o40 coloured by chain, side view.
PDB entry 2o40 coloured by chain, top view.
Source organism: Human immunodeficiency virus 1
Primary publication:
Convergent chemical synthesis and crystal structure of a 203 amino acid "covalent dimer" HIV-1 protease enzyme molecule.
Torbeev VY, Kent SB
Angew Chem Int Ed Engl 46 1667-70 (2007)
PMID: 17397076

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
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128758 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidase A2 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 203 amino acids
Theoretical weight: 21.89 KDa
Source organism: Human immunodeficiency virus 1
Expression system: Not provided
UniProt:
  • Canonical: O38716 (Residues: 1-99; Coverage: 100%)
Gene name: pol
Sequence domains: Retroviral aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:
Ligand 2NC 1 x 2NC
3 modified residues:
Ligand NLE 4 x NLE
Ligand YCM 3 x YCM
Ligand ABA 4 x ABA

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P212121
Unit cell:
a: 51.326Å b: 58.306Å c: 61.699Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.191 0.237
Expression system: Not provided

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Citations

17 review citations

Rethinking amide bond synthesis.
Pattabiraman et al. (2011)
16 more