Super-folder green fluorescent protein artificiall dimer linked via 148 position

Structure

x-ray diffraction · 2 distinct chains · 12% helix, 51% 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 B, A
• DB5 · [(4~{S})-4,5,6,7,8,9-hexahydro-1~{H}-cycloocta[d][1,2, 3]triazol-4-yl] hydrogen carbonate · ligand · chains B, A
• GOL · Glycerol · additive · chains B
• EDO · 1,2-ethanediol · additive · chains B

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

Pockets

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

Interfaces

1 interface between chains.

• B–A · 721 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 cofactor, 2 covalent (chromophore, covalent ligand).

Compared structures

• 5NHN · Super-Folder Green Fluorescent Protein Artificiall dimer linked via 148 position · the same entry in another collection · chain B against B, 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 5NHN · PDBe 5NHN · UniProt A0A059PIQ0