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Helix Bundle Quaternary Structure from alpha/beta-Peptide Foldamers: GCN4-p1 with beta-residues at b and f heptad positions.

Analyse Helix Bundle Quaternary Structure from alpha/beta-Peptide Foldamers: GCN4-p1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2OXJ
Type
protein
Length
95 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2
Molecule
hybrid alpha/beta peptide based on the GCN4-p1 sequence; heptad positions b and f…

Structure

x-ray diffraction · resolution 2 · 2 distinct chains · 91% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
Ahybrid alpha/beta peptide based on the GCN4-p1 sequence; heptad positions b and f substituted with beta-amino acidsprotein3388% helix, 0% strand—
B, Chybrid alpha/beta peptide based on the GCN4-p1 sequence; heptad positions b and f substituted with beta-amino acidsprotein3194% helix, 0% strand—

Ligands and binding sites

  • ACT · Acetate ion · additive · chains B

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

Interfaces

3 interfaces between chains.

  • A–C · 791 Ų buried · 4 hydrogen bonds · protein-protein
  • B–C · 724 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 648 Ų buried · 1 hydrogen bond · protein-protein

Modifications

Observed in the structure: 27 modified (nonstandard).

Compared structures

  • 2OXJ · Helix bundle quaternary structure from ALPHA/BETA-peptide foldamers: GCN4-P1 with… · the same entry in another collection · chain A against A, TM-score 0.88

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