Guinea pig N-acylethanolamine-hydrolyzing acid amidase (naaa) covalently bound to beta-lactam inhibitor ARN726

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 25% strand (DSSP).

Ligands and binding sites

• HJA · (2S)-3-amino-2-{[(4-cyclohexylbutoxy) carbonyl]amino}propanethioic S-acid · ligand · 2 copies · chains A, B, C, D
• NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A, B, C, D
• CL · Chloride ion · ion · 11 copies · chains A, B, C, D
• PO4 · Phosphate ion · ion · 2 copies · chains B, D

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

Pockets

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

Interfaces

6 interfaces between chains.

• A–B · 2082 Ų buried · 24 hydrogen bonds · protein-protein
• C–D · 2004 Ų buried · 26 hydrogen bonds · protein-protein
• A–D · 284 Ų buried · 2 hydrogen bonds · protein-protein
• B–C · 220 Ų buried · 0 hydrogen bonds · protein-protein
• A–C · 130 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 glycan, 2 covalent (N-glycosylation, covalent ligand).

Compared structures

• 6DY2 · Guinea pig N-acylethanolamine-hydrolyzing acid amidase (NAAA) covalently bound to… · the same entry in another collection · chain A against A, TM-score 1.00
• H0VCJ6 · AlphaFold monomer V2.0 prediction for N-acylethanolamine-hydrolyzing acid amidase (H0VCJ6) · a predicted model of the same protein · chain B against A, TM-score 0.98

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 H0VCJ6
• Elsewhere: RCSB PDB 6DY2 · PDBe 6DY2 · UniProt H0VCJ6