Structure of a triclinic crystal of the fimh lectin domain in complex with a propynyl biphenyl alpha-D-mannoside, at 1.4 a resolution

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 51% strand (DSSP).

Ligands and binding sites

• FYZ · (2R,3S,4S,5S,6S)-2-(hydroxymethyl)-6-[3-(4-phenylphenyl)prop-2-ynoxy]oxane-3,4,5-triol · ligand · 4 copies · chains A, B, C, D
• SO4 · Sulfate ion · ion · 3 copies · chains A

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

Pockets

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

Interfaces

5 interfaces between chains.

• A–B · 595 Ų buried · 7 hydrogen bonds · protein-protein
• B–C · 428 Ų buried · 10 hydrogen bonds · protein-protein
• B–D · 379 Ų buried · 5 hydrogen bonds · protein-protein
• A–D · 364 Ų buried · 3 hydrogen bonds · protein-protein
• A–C · 223 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

• 4AV5 · Structure of a triclinic crystal of the FimH lectin domain in complex with a propynyl… · 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 A2IC68
• Elsewhere: RCSB PDB 4AV5 · PDBe 4AV5 · UniProt A2IC68