E. COLI P pilus chaperone-subunit complex papd-paph bound to pilus biogenesis inhibitor, pilicide 5D

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 45% strand (DSSP).

Ligands and binding sites

• EC2 · (2R,3R)-8-cyclopropyl-7-(naphthalen-1-ylmethyl)-5-oxo-2-phenyl-2,3-dihydro-5H-[1,3]thiazolo[3,2-a]pyridine-3-carboxylic acid · ligand · chains A
• EC5 · (2R)-2-[5-cyclopropyl-6-(hydroxysulfanyl)-4-(naphthalen-1-ylmethyl)-2-oxopyridin-1(2H)-yl]-3-phenylpropanoic acid · ligand · chains A
• CO · Cobalt (II) ion · metal · chains B
• GOL · Glycerol · additive · chains A, B
• PGO · S-1,2-propanediol · additive · chains B

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

Pockets

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

Interfaces

1 interface between chains.

• A–B · 2018 Ų buried · 42 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

• 2XG5 · E. coli P pilus chaperone-subunit complex PapD-PapH bound to pilus biogenesis inhibitor… · the same entry in another collection · chain A against A, TM-score 1.00
• P15319 · AlphaFold monomer V2.0 prediction for chaperone protein papd (P15319) · a predicted model of the same protein · chain A against A, TM-score 0.99
• P07111 · AlphaFold monomer V2.0 prediction for pap fimbrial minor pilin protein (P07111) · a predicted model of the same protein · chain B against A, TM-score 0.97

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 P15319
• Every structure of UniProt P07111
• Elsewhere: RCSB PDB 2XG5 · PDBe 2XG5 · UniProt P15319 · UniProt P07111