The structural and biochemical characterization of acyl-CoA hydrolase from staphylococcus aureus in complex with butyryl coenzyme a, coenzyme a, and coenzyme a disulfide

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 40% strand (DSSP).

Ligands and binding sites

• BCO · Butyryl Coenzyme A · ligand · chains A, B
• COA · Coenzyme A · ligand · chains A, B
• 5NG · [[(2~{S},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl] [(3~{R})-4-[[3-[2-[2-[3-[[(2~{R})-4-[[[(2~{R},3~{S},4~{R},5~{R})-5-(6-aminopurin-9-yl)-4-oxidanyl-3-phosphonooxy-oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxy-3,3-dimethyl-2-oxidanyl-butanoyl]amino]propanoylamino]ethyldisulfanyl ]ethylamino]-3-oxidanylidene-propyl]amino]-2,2-dimethyl-3-oxidanyl-4-oxidanylidene-butyl] hydrogen phosphate · ligand · chains A, B, C

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

Pockets

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

Interfaces

3 interfaces between chains.

• A–B · 1893 Ų buried · 21 hydrogen bonds · protein-protein
• B–C · 769 Ų buried · 8 hydrogen bonds · protein-protein
• A–C · 226 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

• 5EGL · The structural and biochemical characterization of acyl-coa hydrolase from Staphylococcus… · 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 A0A0H3K033
• Elsewhere: RCSB PDB 5EGL · PDBe 5EGL · UniProt A0A0H3K033