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Helix bundle quaternary structure from ALPHA/BETA-peptide foldamers: GCN4-pli with beta-residues at B and F heptad positions.

Analyse Helix bundle quaternary structure from ALPHA/BETA-peptide foldamers: GCN4-pli… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2OXK
Type
protein
Length
33 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hybrid ALPHA/BETA peptide based on the GCN4-pli sequence
Ligands
ACE

Structure

x-ray diffraction · 1 distinct chain · 85% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHybrid ALPHA/BETA peptide based on the GCN4-pli sequenceprotein3385% helix, 0% strand—

Ligands and binding sites

  • ACE · Acetyl group · ligand · chains A
  • FMT · Formic acid · additive · 5 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Modifications

Observed in the structure: 9 modified, 1 covalent (nonstandard, covalent ligand).

Compared structures

  • 2OXK · Helix Bundle Quaternary Structure from alpha/beta-Peptide Foldamers: GCN4-pLI with… · the same entry in another collection · chain A against A, TM-score 0.88

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