Rabbit N-acylethanolamine-hydrolyzing acid amidase (naaa) in complex with non-covalent benzothiazole-piperazine inhibitor ARN19702, in presence of triton X-100

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 26% strand (DSSP).

Ligands and binding sites

• TRT · Fragment of triton X-100 · ligand · 2 copies · chains A, B
• 27L · 4-(2,4,4-trimethylpentan-2-yl)phenol · ligand · chains A, B
• WTF · [2-(ethylsulfonyl)phenyl][(2S)-4-(6-fluoro-1,3-benzothiazol-2-yl)-2-methylpiperazin-1-yl]methanone · ligand · chains A, B
• TON · 2-{2-[4-(1,1,3,3-tetramethylbutyl) phenoxy]ethoxy}ethanol · ligand · chains B
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B
• K · Potassium ion · metal · chains A

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 1954 Ų buried · 25 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 glycan (N-glycosylation).

Compared structures

• 6DXZ · Rabbit N-acylethanolamine-hydrolyzing acid amidase (NAAA) in complex with non-covalent… · the same entry in another collection · chain A against A, TM-score 1.00
• G1T7U7 · AlphaFold monomer V2.0 prediction for N-acylethanolamine-hydrolyzing acid amidase (G1T7U7) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 G1T7U7
• Elsewhere: RCSB PDB 6DXZ · PDBe 6DXZ · UniProt G1T7U7