Crystal structures of highly constrained substrate and hydrolysis products bound to HIV-1 protease. implications for catalytic mechanism

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 55% strand (DSSP).

Ligands and binding sites

• DRS · (9S,12S)-9-(1-methylethyl)-7,10-dioxo-2-oxa-8,11-diazabicyclo[12.2.2]octadeca-1(16),14,17-triene-12-carboxylic acid · ligand · 2 copies · chains A, B
• SO4 · Sulfate ion · ion · 3 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 1821 Ų buried · 41 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (nonstandard).

Compared structures

• 3BXS · Crystal Structures Of Highly Constrained Substrate And Hydrolysis Products Bound To HIV-1… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P03369
• Elsewhere: RCSB PDB 3BXS · PDBe 3BXS · UniProt P03369