Crystal structure of HTLV protease complexed with the inhibitor, kni- 10562

Structure

x-ray diffraction · 1 distinct chain · 8% helix, 41% strand (DSSP).

Ligands and binding sites

• E13 · N-[(2S,3S)-4-{(4R)-4-[(2,2-dimethylpropyl)carbamoyl]-5,5-dimethyl-1,3-thiazolidin-3-yl}-3-hydroxy-4-oxo-1-phenylbutan-2-yl]-N~2~-{(2S)-2-[(methoxycarbonyl)amino]-2-phenylacetyl}-3-methyl-L-valinamide · ligand · 6 copies · chains A, B, C, D, E, F, G, H, I, J, K, L

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

Pockets

12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Interfaces

15 interfaces between chains.

• K–L · 1986 Ų buried · 29 hydrogen bonds · protein-protein
• A–B · 1984 Ų buried · 28 hydrogen bonds · protein-protein
• I–J · 1983 Ų buried · 29 hydrogen bonds · protein-protein
• C–D · 1973 Ų buried · 31 hydrogen bonds · protein-protein
• G–H · 1968 Ų buried · 32 hydrogen bonds · protein-protein

Compared structures

• 3LIN · crystal structure of HTLV protease complexed with the inhibitor, KNI-10562 · the same entry in another collection · chain B against B, 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 Q82134
• Elsewhere: RCSB PDB 3LIN · PDBe 3LIN · UniProt Q82134