Aspergillus niger ferulic acid decarboxylase (fdc) E282Q variant in complex with the covalent adduct formed between prfmn cofactor and cinnamic acid (INT2)

Structure

x-ray diffraction · 1 distinct chain.

Ligands and binding sites

• JQK · [(2~{R},3~{S},4~{S})-2,3,4-tris(oxidanyl)-5-[(16~{R})-11,12,14,14-tetramethyl-5-oxidanyl-3-oxidanylidene-16-(2-phenylethyl)-1,4,6,8-tetrazatetracyclo[7.7.1.0^{2, 7}.0^{13,17}]heptadeca-2(7),5,9(17),10,12-pentaen-8-yl]pentyl] dihydrogen phosphate · ligand · chains A
• K · Potassium ion · metal · 2 copies · chains A
• MN · Manganese (II) ion · metal · chains A

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

Compared structures

• 6R3F · Aspergillus niger ferulic acid decarboxylase (Fdc) E282Q variant in complex with the… · the same entry in another collection · chain A against A, TM-score 1.00
• A2QHE5 · AlphaFold monomer V2.0 prediction for ferulic acid decarboxylase 1 (A2QHE5) · a predicted model of the same protein · chain A 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 A2QHE5
• Elsewhere: RCSB PDB 6R3F · PDBe 6R3F · UniProt A2QHE5