Structure of leucyl aminopeptidase from trypanosoma brucei in complex with bestatin

Structure

x-ray diffraction · 3 distinct chains · 38% helix, 22% strand (DSSP).

Ligands and binding sites

• BES · 2-(3-amino-2-hydroxy-4-phenyl-butyrylamino)-4-methyl-pentanoic acid · ligand · 12 copies · chains A, B, D, C, E, F, G, H, I, J, K, L
• BCT · Bicarbonate ion · ligand · 12 copies · chains A, B, D, C, E, F, G, H, I, J, K, L
• MN · Manganese (II) ion · metal · 24 copies · chains A, B, D, C, E, F, G, H, I, J, K, L
• SO4 · Sulfate ion · ion · 11 copies · chains A, E, B, C, D, F, G, H, I, J, K, L
• EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · 3 copies · chains A, C, L, E

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Interfaces

25 interfaces between chains.

• B–C · 1622 Ų buried · 37 hydrogen bonds · protein-protein
• D–F · 1586 Ų buried · 35 hydrogen bonds · protein-protein
• A–E · 1575 Ų buried · 36 hydrogen bonds · protein-protein
• J–K · 1281 Ų buried · 26 hydrogen bonds · protein-protein
• J–L · 1278 Ų buried · 25 hydrogen bonds · protein-protein

Compared structures

• 5NTD · Structure of Leucyl aminopeptidase from Trypanosoma brucei in complex with Bestatin · 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 Q385B0
• Elsewhere: RCSB PDB 5NTD · PDBe 5NTD · UniProt Q385B0