Switching GFP fluorescence using genetically encoded phenyl azide chemistry through two different non-native post-translational modifications routes at the same position.

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 52% strand (DSSP).

Ligands and binding sites

• CRO · {2-[(1R,2R)-1-amino-2-hydroxypropyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid · ligand · 2 copies · chains A, B
• SO4 · Sulfate ion · ion · 11 copies · chains A, B
• GOL · Glycerol · additive · 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, 4 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 664 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 cofactor, 2 modified (chromophore, nonstandard).

Compared structures

• 5BTT · Switching GFP fluorescence using genetically encoded phenyl azide chemistry through two… · 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 A0A059PIQ0
• Elsewhere: RCSB PDB 5BTT · PDBe 5BTT · UniProt A0A059PIQ0