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ALPHA/BETA-peptide helix bundles: the GCN4-pli side chain sequence on an (alpha-alpha-alpha-beta) backbone

Analyse ALPHA/BETA-peptide helix bundles: the GCN4-pli side chain sequence on an… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3C3F
Type
protein
Length
124 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ALPHA/BETA peptide with the GCN4-pli side chain sequence on an (alpha-alpha-alpha-beta)…
Ligands
ACE

Structure

x-ray diffraction · 1 distinct chain · 94% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DALPHA/BETA peptide with the GCN4-pli side chain sequence on an (alpha-alpha-alpha-beta) backboneprotein3194% helix, 0% strand—

Ligands and binding sites

  • ACE · Acetyl group · ligand · 4 copies · chains A, B, C, D

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

Interfaces

6 interfaces between chains.

  • A–D · 857 Ų buried · 4 hydrogen bonds · protein-protein
  • C–D · 837 Ų buried · 2 hydrogen bonds · protein-protein
  • A–B · 836 Ų buried · 4 hydrogen bonds · protein-protein
  • B–C · 827 Ų buried · 3 hydrogen bonds · protein-protein
  • A–C · 90 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 32 modified, 4 covalent (nonstandard, covalent ligand).

Compared structures

  • 3C3F · alpha/beta-Peptide helix bundles: The GCN4-pLI side chain sequence on an… · the same entry in another collection · chain B against B, TM-score 0.89

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