Structure of wild type a. niger FDC1 that has been illuminated with UV light, with prfmn in the iminium and ketimine form

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 23% strand (DSSP).

Ligands and binding sites

• 4LU · 1-deoxy-5-O-phosphono-1-(3,3,4,5-tetramethyl-9,11-dioxo-2,3,8,9,10,11-hexahydro-7H-quinolino[1,8-fg]pteridin-12-ium-7-yl)-D-ribitol · ligand · chains A
• FZZ · 1-deoxy-5-O-phosphono-1-[(10AR)-2,2,3,4-tetramethyl-8, 10-dioxo-1,2,8,9,10,10A-hexahydro-6H-indeno[1,7-ef]pyrimido[4,5-b][1,4]diazepin-6-yl]-D-ribitol · 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.

Pockets

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

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

• 6EV3 · Structure of wild type A. niger Fdc1 that has been illuminated with UV light, with prFMN… · 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 6EV3 · PDBe 6EV3 · UniProt A2QHE5