Crystal structure of the E192N mutant of E. COLI N- acetylneuraminic acid lyase in complex with pyruvate and the inhibitor (2R,3R)-2,3,4-trihydroxy-N,N- dipropylbutanamide in space group P21 crystal form I

Structure

x-ray diffraction · 2 distinct chains · 54% helix, 13% strand (DSSP).

Ligands and binding sites

• ZZI · (2R,3R)-2,3,4-trihydroxy-N,N-dipropylbutanamide · ligand · 4 copies · chains A, C, B, D

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

Pockets

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

Interfaces

4 interfaces between chains.

• B–C · 1246 Ų buried · 12 hydrogen bonds · protein-protein
• A–D · 1245 Ų buried · 12 hydrogen bonds · protein-protein
• A–C · 1068 Ų buried · 13 hydrogen bonds · protein-protein
• B–D · 1052 Ų buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (nonstandard).

Compared structures

• 2WPB · Crystal structure of the E192N mutant of E. Coli N-acetylneuraminic acid lyase in complex… · the same entry in another collection · chain A against A, TM-score 1.00
• P0A6L4 · AlphaFold monomer V2.0 prediction for N-acetylneuraminate lyase (P0A6L4) · a predicted model of the same protein · chain B 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 P0A6L4
• Elsewhere: RCSB PDB 2WPB · PDBe 2WPB · UniProt P0A6L4