The structure of a CoA-dependent acyl-homoserine lactone synthase, rpai, with the adduct of sah and P-coumaroyl CoA

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 26% strand (DSSP).

Ligands and binding sites

• COA · Coenzyme A · ligand · 2 copies · chains A, B
• U4Y · (2S)-4-({[(2S,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-3,4-dihydroxytetrahydrofuran-2-yl]methyl}sulfanyl)-2-{[(2E)-3-(cis-4-hydroxycyclohexa-2,5-dien-1-yl)prop-2-enoyl]amino}butanoic acid · ligand · 2 copies · chains A, B

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

1 interface between chains.

• A–B · 452 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

• 6WN0 · The structure of a CoA-dependent acyl-homoserine lactone synthase, RpaI, with the adduct… · the same entry in another collection · chain B against B, TM-score 1.00
• Q6NCZ6 · AlphaFold monomer V2.0 prediction for 4-coumaroyl-homoserine lactone synthase (Q6NCZ6) · 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 Q6NCZ6
• Elsewhere: RCSB PDB 6WN0 · PDBe 6WN0 · UniProt Q6NCZ6