GL1X · GenesisL1 explorer

Ligand · W35

W35 · 5-(5-(4-(4,5-dihydro-2-oxazoly)phenoxy)pentyl)-3-methyl isoxazole

W35, 5-(5-(4-(4,5-dihydro-2-oxazoly)phenoxy)pentyl)-3-methyl isoxazole (C18 H22 N2 O3, 314.4 g/mol), in the MolNFT structures on GenesisL1: bound in 8 records (4 PDB entries). Every binding site with its residues within 4.5 Å, the residues…

Component
W35
Formula
C18 H22 N2 O3
Class
ligand
Structures
8
PDB entries
4

Binding sites

W35 in 8 structures; the first of them:

  • 1RUC · Rhinovirus 14 mutant N1105S complexed with antiviral compound win 52035 · W35 1290 · binds ILE104, SER105, LEU106, PHE124, SER126, TYR128, ALA150, TYR152 and 10 more
  • 1RUE · Rhinovirus 14 site directed mutant N1219A complexed with antiviral compound win 52035 · W35 1290 · binds ILE104, LEU106, SER126, TYR128, ALA150, TYR152, PRO174, SER175 and 8 more
  • 1RUG · Rhinovirus 14 mutant N1219S complexed with antiviral compound win 52035 · W35 1290 · binds ILE104, ASN105, LEU106, PHE124, SER126, TYR128, ALA150, TYR152 and 11 more
  • 2R06 · Structural analysis of antiviral agents that interact with the capsid of human… · W35 1900 · binds ILE104, ASN105, LEU106, PHE124, SER126, TYR128, ALA150, TYR152 and 11 more
  • 1RUC · Rhinovirus 14 mutant N1105S complexed with antiviral compound win 52035 · W35 1290 · binds ILE104, SER105, LEU106, PHE124, SER126, TYR128, ALA150, TYR152 and 10 more
  • 1RUE · Rhinovirus 14 site directed mutant N1219A complexed with antiviral compound win 52035 · W35 1290 · binds ILE104, LEU106, SER126, TYR128, ALA150, TYR152, PRO174, SER175 and 8 more
  • 1RUG · Rhinovirus 14 mutant N1219S complexed with antiviral compound win 52035 · W35 1290 · binds ILE104, ASN105, LEU106, PHE124, SER126, TYR128, ALA150, TYR152 and 11 more
  • 2R06 · Structural analysis of antiviral agents that interact with the capsid of human… · W35 1900 · binds ILE104, ASN105, LEU106, PHE124, SER126, TYR128, ALA150, TYR152 and 11 more

Residues it binds most

TYR 8, VAL 8, SER 8, ALA 8, MET 8, PHE 8, ILE 8, LEU 8, PRO 8, ASN 4 (residue and the binding sites it lines).

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