Research workbench
Cyclic residues in ALPHA/BETA-peptide helix bundles: GCN4-pli side chain sequence on an (alpha-alpha-beta) backbone with a cyclic beta- residue at position 10
Analyse Cyclic residues in ALPHA/BETA-peptide helix bundles: GCN4-pli side chain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3HET
- Type
- protein
- Length
- 60 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ALPHA/BETA-peptide based on the GCN4-pli side chain sequence with an (alpha-alpha-beta)…
- Ligands
- BAL
Structure
x-ray diffraction · 1 distinct chain · 93% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | ALPHA/BETA-peptide based on the GCN4-pli side chain sequence with an (alpha-alpha-beta) backbone and a cyclic beta- residue at position 10 | protein | 30 | 93% helix, 0% strand | — |
Ligands and binding sites
- BAL · Beta-alanine · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 56 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 20 modified, 2 covalent (nonstandard, covalent ligand).
Compared structures
- 3HET · Cyclic residues in alpha/beta-peptide helix bundles: GCN4-pLI side chain sequence on an… · the same entry in another collection · chain B against B, TM-score 0.84
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 3HET · PDBe 3HET
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