Kinetics, stability, and structural changes in high resolution crystal structures of HIV-1 protease with drug resistant mutations L24I, I50V, and G73S

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 56% strand (DSSP).

Ligands and binding sites

• MK1 · N-[2(R)-hydroxy-1(S)-indanyl]-5-[(2(S)-tertiary butylaminocarbonyl)-4(3-pyridylmethyl)piperazino]-4(S)-hydroxy-2(R)-phenylmethylpentanamide · ligand · 2 copies · chains A, B, D, E
• CL · Chloride ion · ion · 2 copies · chains B, D
• ACY · Acetic acid · additive · 3 copies · chains A, B, E

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Interfaces

5 interfaces between chains.

• A–B · 1829 Ų buried · 35 hydrogen bonds · protein-protein
• D–E · 1791 Ų buried · 37 hydrogen bonds · protein-protein
• B–E · 290 Ų buried · 4 hydrogen bonds · protein-protein
• A–D · 147 Ų buried · 1 hydrogen bond · protein-protein
• B–D · 72 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

• 2AVV · Kinetics, stability, and structural changes in high resolution crystal structures of… · 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 P04587
• Elsewhere: RCSB PDB 2AVV · PDBe 2AVV · UniProt P04587