Crystal structure analysis of a single amino acid deletion mutation in egfp

Structure

x-ray diffraction · 1 distinct chain · 10% 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 · chains A
• SO4 · Sulfate ion · ion · 2 copies · chains A
• EDO · 1,2-ethanediol · additive · 16 copies · chains A
• TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 3 copies · chains A

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

Pockets

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

Modifications

Observed in the structure: 2 cofactor, 1 covalent (chromophore, additive adduct).

Compared structures

• 4KAG · Crystal structure analysis of a single amino acid deletion mutation in EGFP · the same entry in another collection · chain A against A, TM-score 1.00
• P42212 · AlphaFold monomer V2.0 prediction for green fluorescent protein (P42212) · 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 P42212
• Elsewhere: RCSB PDB 4KAG · PDBe 4KAG · UniProt P42212