Enah EVH1 in complex with ac-[2-cl-F]-pp-[prom-1]-NH2

Structure

x-ray diffraction · 3 distinct chains · 17% helix, 49% strand (DSSP).

Ligands and binding sites

• ACE · Acetyl group · ligand · 3 copies · chains B, A, C, E
• 2L5 · 2-chloro-L-phenylalanine · ligand · 3 copies · chains B, A, C, D, E
• 92B · (3~{S},7~{R},10~{R},13~{S})-2-oxidanylidene-1,4-diazatricyclo[8.3.0.0^{3,7}]tridec-8-ene-13-carboxylic acid · ligand · 3 copies · chains B, C, D, A, E
• NH2 · Amino group · ion · 3 copies
• CL · Chloride ion · ion · chains B

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

5 interfaces between chains.

• B–A · 521 Ų buried · 11 hydrogen bonds · protein-protein
• B–C · 141 Ų buried · 3 hydrogen bonds · protein-protein
• A–E · 135 Ų buried · 3 hydrogen bonds · protein-protein
• B–D · 123 Ų buried · 4 hydrogen bonds · protein-protein
• A–C · 26 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 covalent (covalent ligand).

Compared structures

• 5N9P · ENAH EVH1 in complex with Ac-[2-Cl-F]-PP-[ProM-1]-NH2 · the same entry in another collection · chain B against B, 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 0.98

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 5N9P · PDBe 5N9P · UniProt Q8N8S7