Ef-tu (escherichia COLI) complexed with nvp-LDU796

Structure

x-ray diffraction · 2 distinct chains · 21% helix, 37% strand (DSSP).

Ligands and binding sites

• 05N · (3R,4R)-4-hydroxy-3-methyl-L-proline · ligand · chains A, I
• GDP · Guanosine-5'-diphosphate · ligand · chains A
• MG · Magnesium ion · metal · 2 copies · chains A
• NH2 · Amino group · ion · chains A, I
• SO4 · Sulfate ion · ion · 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.

Interfaces

1 interface between chains.

• A–I · 507 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified, 2 covalent (nonstandard, covalent ligand).

Compared structures

• 4G5G · ef-tu (Escherichia coli) complexed with nvp-ldu796 · the same entry in another collection · chain A against A, TM-score 1.00
• P0CE47 · AlphaFold monomer V2.0 prediction for elongation factor tu 1 (P0CE47) · a predicted model of the same protein · chain A against A, TM-score 0.60

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 P0CE47
• Elsewhere: RCSB PDB 4G5G · PDBe 4G5G · UniProt P0CE47