Enah EVH1 in complex with ac-[2-cl-F]-pppptedel-NH2

Structure

x-ray diffraction · 4 distinct chains · 17% helix, 46% strand (DSSP).

Ligands and binding sites

• ACE · Acetyl group · ligand · 2 copies · chains A, B, J
• 2L5 · 2-chloro-L-phenylalanine · ligand · 2 copies · chains A, I, B, J
• NO3 · Nitrate ion · ion · 6 copies · chains A, B
• NH2 · Amino group · ion · chains J
• 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, 0 with a druggability of 0.5 or more.

Interfaces

3 interfaces between chains.

• B–J · 409 Ų buried · 5 hydrogen bonds · protein-protein
• A–B · 367 Ų buried · 12 hydrogen bonds · protein-protein
• A–I · 242 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

• 5NC2 · ENAH EVH1 in complex with Ac-[2-Cl-F]-PPPPTEDEL-NH2 · the same entry in another collection · chain A against A, TM-score 1.00
• Q8N8S7 · AlphaFold monomer V2.0 prediction for protein enabled homolog (Q8N8S7) · a predicted model of the same protein · chain B 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 Q8N8S7
• Elsewhere: RCSB PDB 5NC2 · PDBe 5NC2 · UniProt Q8N8S7