Crystal structure analysis of single amino acid deletion mutations in egfp

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 50% 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
• NA · Sodium ion · metal · 2 copies · chains A
• ZN · Zinc ion · metal · 2 copies · chains A
• EDO · 1,2-ethanediol · additive · 9 copies · chains A
• EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A

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

Pockets

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

Modifications

Observed in the structure: 2 cofactor (chromophore).

Compared structures

• 4KA9 · Crystal structure analysis of single amino acid deletion mutations 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 4KA9 · PDBe 4KA9 · UniProt P42212