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Enah EVH1 in complex with ac-[2-cl-F]-pp-[prom-9]-oh

Analyse Enah EVH1 in complex with ac-[2-cl-F]-pp-[prom-9]-oh in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5NBX
Type
protein
Length
221 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein enabled homolog
UniProt
Q8N8S7
Ligands
PRO, 2L5, 8SN, BR
Pockets
1 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 18% helix, 50% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein enabled homologprotein10918% helix, 49% strandQ8N8S7
BProtein enabled homologprotein11218% helix, 51% strandQ8N8S7

Ligands and binding sites

  • PRO · Proline · ligand · 4 copies · chains A, B
  • 2L5 · 2-chloro-L-phenylalanine · ligand · 2 copies · chains A, B
  • 8SN · (3~{S},7~{R},10~{R},11~{R},13~{S})-11-methyl-2-oxidanylidene-1,4-diazatricyclo[8.3.0.0^{3,7}]tridec-8-ene-13-carboxylic acid · ligand · 2 copies · chains A, B
  • BR · Bromide ion · ion · chains A
  • ACY · Acetic acid · additive · 2 copies · chains A, 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12080.460.74242L5, PRO, ACY

Interfaces

1 interface between chains.

  • A–B · 527 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 5NBX · ENAH EVH1 in complex with Ac-[2-Cl-F]-PP-[ProM-9]-OH · 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 A against A, TM-score 0.98

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